GUX1_ARATH
ID GUX1_ARATH Reviewed; 659 AA.
AC Q9LSB1; Q940B5;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=UDP-glucuronate:xylan alpha-glucuronosyltransferase 1;
DE Short=UDP-GlcA:xylan glucuronyltransferase 1;
DE EC=2.4.1.-;
DE AltName: Full=Glycogenin-like protein 1;
DE AltName: Full=Plant glycogenin-like starch initiation protein 1;
DE AltName: Full=Protein GLUCURONIC ACID SUBSTITUTION OF XYLAN 1;
DE Short=AtGUX1;
GN Name=GUX1; Synonyms=PGSIP1; OrderedLocusNames=At3g18660; ORFNames=MVE11.2;
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] (ISOFORM 1), AND GENE FAMILY.
RX AGRICOLA=IND43669941;
RA Chatterjee M., Berbezy P., Vyas D., Coates S., Barsby T.;
RT "Reduced expression of a protein homologous to glycogenin leads to
RT reduction of starch content in Arabidopsis leaves.";
RL Plant Sci. 168:501-509(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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] (ISOFORM 2).
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21124849; DOI=10.1371/journal.pone.0015481;
RA Oikawa A., Joshi H.J., Rennie E.A., Ebert B., Manisseri C.,
RA Heazlewood J.L., Scheller H.V.;
RT "An integrative approach to the identification of Arabidopsis and rice
RT genes involved in xylan and secondary wall development.";
RL PLoS ONE 5:E15481-E15481(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20852069; DOI=10.1073/pnas.1005456107;
RA Mortimer J.C., Miles G.P., Brown D.M., Zhang Z., Segura M.P., Weimar T.,
RA Yu X., Seffen K.A., Stephens E., Turner S.R., Dupree P.;
RT "Absence of branches from xylan in Arabidopsis gux mutants reveals
RT potential for simplification of lignocellulosic biomass.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:17409-17414(2010).
CC -!- FUNCTION: Glycosyltransferase required for the addition of both
CC glucuronic acid and 4-O-methylglucuronic acid branches to xylan in stem
CC cell walls. In association with GUX2, is responsible for almost all of
CC the substitutions of the xylan backbone in stem glucuronoxylan.
CC {ECO:0000269|PubMed:20852069, ECO:0000269|PubMed:21124849}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P46976};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:20852069, ECO:0000305|PubMed:21124849}; Single-pass
CC type II membrane protein {ECO:0000305|PubMed:20852069,
CC ECO:0000305|PubMed:21124849}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LSB1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LSB1-2; Sequence=VSP_042766;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants show reduced xylan substitution.
CC {ECO:0000269|PubMed:20852069}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin
CC subfamily. {ECO:0000305}.
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DR EMBL; AY749109; AAU93699.1; -; mRNA.
DR EMBL; AB026654; BAB01792.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76127.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76128.1; -; Genomic_DNA.
DR EMBL; AY056133; AAL07212.1; -; mRNA.
DR EMBL; AY142690; AAN13228.1; -; mRNA.
DR RefSeq; NP_001030722.1; NM_001035645.3. [Q9LSB1-1]
DR RefSeq; NP_566615.1; NM_112752.3. [Q9LSB1-2]
DR AlphaFoldDB; Q9LSB1; -.
DR SMR; Q9LSB1; -.
DR BioGRID; 6730; 1.
DR IntAct; Q9LSB1; 1.
DR STRING; 3702.AT3G18660.2; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR PaxDb; Q9LSB1; -.
DR PRIDE; Q9LSB1; -.
DR ProteomicsDB; 230119; -. [Q9LSB1-1]
DR EnsemblPlants; AT3G18660.1; AT3G18660.1; AT3G18660. [Q9LSB1-2]
DR EnsemblPlants; AT3G18660.2; AT3G18660.2; AT3G18660. [Q9LSB1-1]
DR GeneID; 821397; -.
DR Gramene; AT3G18660.1; AT3G18660.1; AT3G18660. [Q9LSB1-2]
DR Gramene; AT3G18660.2; AT3G18660.2; AT3G18660. [Q9LSB1-1]
DR KEGG; ath:AT3G18660; -.
DR Araport; AT3G18660; -.
DR TAIR; locus:2094014; AT3G18660.
DR eggNOG; KOG1950; Eukaryota.
DR InParanoid; Q9LSB1; -.
DR PhylomeDB; Q9LSB1; -.
DR BioCyc; ARA:AT3G18660-MON; -.
DR PRO; PR:Q9LSB1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSB1; baseline and differential.
DR Genevisible; Q9LSB1; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA:TAIR.
DR GO; GO:0080116; F:glucuronoxylan glucuronosyltransferase activity; IMP:TAIR.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0010417; P:glucuronoxylan biosynthetic process; IMP:TAIR.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IGI:TAIR.
DR GO; GO:0045492; P:xylan biosynthetic process; IDA:TAIR.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Golgi apparatus; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..659
FT /note="UDP-glucuronate:xylan alpha-glucuronosyltransferase
FT 1"
FT /id="PRO_0000416733"
FT TRANSMEM 70..90
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 416..418
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 416
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 418
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 445..447
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 472..476
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 526..531
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 526
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT SITE 400
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT VAR_SEQ 105..108
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_042766"
SQ SEQUENCE 659 AA; 76285 MW; E10EF4859FAA3149 CRC64;
MANSPAAPAP TTTTGGDSRR RLSASIEAIC KRRFRRNSKG GGRSDMVKPF NIINFSTQDK
NSSCCCFTKF QIVKLLLFIL LSATLFTIIY SPEAYHHSLS HSSSRWIWRR QDPRYFSDLD
INWDDVTKTL ENIEEGRTIG VLNFDSNEIQ RWREVSKSKD NGDEEKVVVL NLDYADKNVT
WDALYPEWID EEQETEVPVC PNIPNIKVPT RRLDLIVVKL PCRKEGNWSR DVGRLHLQLA
AATVAASAKG FFRGHVFFVS RCFPIPNLFR CKDLVSRRGD VWLYKPNLDT LRDKLQLPVG
SCELSLPLGI QDRPSLGNPK REAYATILHS AHVYVCGAIA AAQSIRQSGS TRDLVILVDD
NISGYHRSGL EAAGWQIRTI QRIRNPKAEK DAYNEWNYSK FRLWQLTDYD KIIFIDADLL
ILRNIDFLFS MPEISATGNN GTLFNSGVMV IEPCNCTFQL LMEHINEIES YNGGDQGYLN
EVFTWWHRIP KHMNFLKHFW IGDEDDAKRK KTELFGAEPP VLYVLHYLGM KPWLCYRDYD
CNFNSDIFVE FATDIAHRKW WMVHDAMPQE LHQFCYLRSK QKAQLEYDRR QAEAANYADG
HWKIRVKDPR FKICIDKLCN WKSMLRHWGE SNWTDYESFV PTPPAITVDR RSSLPGHNL
