XG113_ARATH
ID XG113_ARATH Reviewed; 644 AA.
AC Q8VXZ5; B9DFT3; Q9ZQN4;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Arabinosyltransferase XEG113 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000305};
DE AltName: Full=Protein LATERAL ROOT DEVELOPMENT 5 {ECO:0000303|PubMed:24619997};
DE AltName: Full=Xyloglucanase 113 {ECO:0000303|PubMed:19667208};
GN Name=XEG113 {ECO:0000303|PubMed:19667208};
GN Synonyms=LRD5 {ECO:0000303|PubMed:24619997};
GN OrderedLocusNames=At2g35610 {ECO:0000312|Araport:AT2G35610};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=24905498; DOI=10.1111/tpj.12577;
RA Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for functional genomics.";
RL Plant J. 79:517-529(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=19667208; DOI=10.1073/pnas.0905434106;
RA Gille S., Haensel U., Ziemann M., Pauly M.;
RT "Identification of plant cell wall mutants by means of a forward chemical
RT genetic approach using hydrolases.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14699-14704(2009).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21680836; DOI=10.1126/science.1206657;
RA Velasquez S.M., Ricardi M.M., Dorosz J.G., Fernandez P.V., Nadra A.D.,
RA Pol-Fachin L., Egelund J., Gille S., Harholt J., Ciancia M., Verli H.,
RA Pauly M., Bacic A., Olsen C.E., Ulvskov P., Petersen B.L., Somerville C.,
RA Iusem N.D., Estevez J.M.;
RT "O-glycosylated cell wall proteins are essential in root hair growth.";
RL Science 332:1401-1403(2011).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=24619997; DOI=10.1093/jxb/eru056;
RA Roycewicz P.S., Malamy J.E.;
RT "Cell wall properties play an important role in the emergence of lateral
RT root primordia from the parent root.";
RL J. Exp. Bot. 65:2057-2069(2014).
RN [9]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=25944827; DOI=10.1104/pp.114.255521;
RA Velasquez S.M., Marzol E., Borassi C., Pol-Fachin L., Ricardi M.M.,
RA Mangano S., Juarez S.P., Salter J.D., Dorosz J.G., Marcus S.E., Knox J.P.,
RA Dinneny J.R., Iusem N.D., Verli H., Estevez J.M.;
RT "Low sugar is not always good: impact of specific o-glycan defects on tip
RT growth in Arabidopsis.";
RL Plant Physiol. 168:808-813(2015).
CC -!- FUNCTION: Plays a role in the arabinosylation of cell wall components.
CC Involved in the arabinosylation of extensin proteins in root hair cells
CC (PubMed:19667208, PubMed:21680836). Extensins are structural
CC glycoproteins present in cell walls and its arabinosylation is
CC important for cell elongation, root hair cell development, lateral root
CC development and root hair tip growth (PubMed:19667208, PubMed:21680836,
CC PubMed:24619997, PubMed:25944827). {ECO:0000269|PubMed:19667208,
CC ECO:0000269|PubMed:21680836, ECO:0000269|PubMed:24619997,
CC ECO:0000269|PubMed:25944827}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:21680836}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:21680836}.
CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC {ECO:0000250|UniProtKB:Q9JI93}.
CC -!- DISRUPTION PHENOTYPE: Increased elongation of hypocotyls
CC (PubMed:19667208). Reduced root hair length (PubMed:21680836). Reduced
CC content of arabinosylated extensins in cell walls (PubMed:19667208,
CC PubMed:21680836). Increased lateral root formation (PubMed:24619997).
CC {ECO:0000269|PubMed:19667208, ECO:0000269|PubMed:21680836,
CC ECO:0000269|PubMed:24619997}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 77 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD15452.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KJ138873; AHL38813.1; -; mRNA.
DR EMBL; AC006068; AAD15452.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09128.1; -; Genomic_DNA.
DR EMBL; AY074327; AAL67023.1; -; mRNA.
DR EMBL; AK316893; BAH19600.1; -; mRNA.
DR PIR; G84770; G84770.
DR RefSeq; NP_850250.1; NM_179919.2.
DR AlphaFoldDB; Q8VXZ5; -.
DR STRING; 3702.AT2G35610.1; -.
DR CAZy; GT77; Glycosyltransferase Family 77.
DR PaxDb; Q8VXZ5; -.
DR PRIDE; Q8VXZ5; -.
DR ProteomicsDB; 242509; -.
DR EnsemblPlants; AT2G35610.1; AT2G35610.1; AT2G35610.
DR GeneID; 818128; -.
DR Gramene; AT2G35610.1; AT2G35610.1; AT2G35610.
DR KEGG; ath:AT2G35610; -.
DR Araport; AT2G35610; -.
DR TAIR; locus:2058769; AT2G35610.
DR eggNOG; ENOG502QSJ9; Eukaryota.
DR HOGENOM; CLU_024474_0_0_1; -.
DR InParanoid; Q8VXZ5; -.
DR OMA; KVEDHPP; -.
DR OrthoDB; 855804at2759; -.
DR PhylomeDB; Q8VXZ5; -.
DR PRO; PR:Q8VXZ5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8VXZ5; baseline and differential.
DR Genevisible; Q8VXZ5; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0052636; F:arabinosyltransferase activity; IMP:TAIR.
DR GO; GO:0052325; P:cell wall pectin biosynthetic process; IMP:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IMP:TAIR.
DR GO; GO:0080147; P:root hair cell development; IMP:TAIR.
DR InterPro; IPR005069; Nucl-diP-sugar_transferase.
DR Pfam; PF03407; Nucleotid_trans; 1.
PE 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..644
FT /note="Arabinosyltransferase XEG113"
FT /id="PRO_0000434540"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..644
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 226..228
FT /note="DXD motif"
FT /evidence="ECO:0000305"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 167
FT /note="M -> V (in Ref. 5; BAH19600)"
FT /evidence="ECO:0000305"
FT CONFLICT 620
FT /note="D -> E (in Ref. 5; BAH19600)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 644 AA; 73213 MW; D436221B732DF780 CRC64;
MVEGWRNGFR DATNSKPLFV TIYATVIIGV LVSSFYVFSA IYSPTNGSSS FLSFPPLSTS
GRIHSLPQEN ATLELPVAPP PPPQALPPPV LEEAQGNSLG KIWVSPPRDK KMPPLETFKL
TKELFGERVK DNVIIVTFGN YAFMDFILTW VKHLTDLDLS NILVGAMDTK LLEALYWKGV
PVFDMGSHMS TVDVGWGSPT FHKMGREKVI LIDSVLPFGY ELLMCDTDMV WLKNPMPYLA
RFPDADVLTS SDQVVPTVID DSLDIWQQVG AAYNIGIFHW RPTESAKKLA KEWKEILLAD
DKVWDQNGFN EIVRRQLGPS VEGDSGLFYA YDGNLKVGIL PASIFCSGHT YFVQAMYQQL
RLEPYAVHTT FQYAGTEGKR HRLREGMVFY DPPEYYDSPG GFIAFKPSIP KSLLLDGKHT
IESHFILVNH QMKQIRSALA IASLLNRTLV MPPIWCRLDR LWFGHPGTLQ GSMTRQPFIC
PLDHVFEVNI MLKELPEEEF GPGIGIREYS FLDNPLLPKQ VKESWLDVQL CQEGKEGCEA
SNNTSPSRVL KFPKRSNEDT FKAIFSSFDD VKVIKFSSIE DAFIGFSDKE REERFRRRVK
RYVGIWCCEE NKTPGHIYYD MYWDEKPGWK PVPPQTPEED HPPL
