GUX2_ARATH
ID GUX2_ARATH Reviewed; 596 AA.
AC Q8GWW4; F4JW13; Q9SZB0; Q9SZB1;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=UDP-glucuronate:xylan alpha-glucuronosyltransferase 2;
DE Short=UDP-GlcA:xylan glucuronyltransferase 2;
DE EC=2.4.1.-;
DE AltName: Full=Glycogenin-like protein 2;
DE AltName: Full=Plant glycogenin-like starch initiation protein 3;
DE AltName: Full=Protein GLUCURONIC ACID SUBSTITUTION OF XYLAN 2;
DE Short=AtGUX2;
GN Name=GUX2; Synonyms=PGSIP3; OrderedLocusNames=At4g33330/At4g33340;
GN ORFNames=F17M5.90/F17M5.100;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP 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 [7]
RP 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 [8]
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 GUX1, is responsible for almost all of
CC the substitutions of the xylan backbone in stem glucuronoxylan.
CC {ECO:0000269|PubMed:20852069}.
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=Q8GWW4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GWW4-2; Sequence=VSP_042767;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB38791.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g33330 and At4g33340.; Evidence={ECO:0000305};
CC Sequence=CAB38792.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g33330 and At4g33340.; Evidence={ECO:0000305};
CC Sequence=CAB80050.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g33330 and At4g33340.; Evidence={ECO:0000305};
CC Sequence=CAB80051.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g33330 and At4g33340.; Evidence={ECO:0000305};
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DR EMBL; AL035678; CAB38791.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL035678; CAB38792.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161583; CAB80050.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161583; CAB80051.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86207.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86208.1; -; Genomic_DNA.
DR EMBL; AK118592; BAC43192.1; -; mRNA.
DR EMBL; BT005924; AAO64859.1; -; mRNA.
DR EMBL; AK175846; BAD43609.1; -; mRNA.
DR EMBL; AK176001; BAD43764.1; -; mRNA.
DR PIR; T05984; T05984.
DR PIR; T05985; T05985.
DR RefSeq; NP_001154284.1; NM_001160812.1. [Q8GWW4-2]
DR RefSeq; NP_195059.3; NM_119487.3. [Q8GWW4-1]
DR AlphaFoldDB; Q8GWW4; -.
DR SMR; Q8GWW4; -.
DR STRING; 3702.AT4G33330.2; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR PaxDb; Q8GWW4; -.
DR PRIDE; Q8GWW4; -.
DR ProteomicsDB; 247153; -. [Q8GWW4-1]
DR EnsemblPlants; AT4G33330.1; AT4G33330.1; AT4G33330. [Q8GWW4-1]
DR EnsemblPlants; AT4G33330.2; AT4G33330.2; AT4G33330. [Q8GWW4-2]
DR GeneID; 829469; -.
DR Gramene; AT4G33330.1; AT4G33330.1; AT4G33330. [Q8GWW4-1]
DR Gramene; AT4G33330.2; AT4G33330.2; AT4G33330. [Q8GWW4-2]
DR KEGG; ath:AT4G33330; -.
DR Araport; AT4G33330; -.
DR TAIR; locus:2119241; AT4G33330.
DR eggNOG; KOG1950; Eukaryota.
DR HOGENOM; CLU_023070_1_0_1; -.
DR InParanoid; Q8GWW4; -.
DR OrthoDB; 1424146at2759; -.
DR PhylomeDB; Q8GWW4; -.
DR PRO; PR:Q8GWW4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GWW4; baseline and differential.
DR Genevisible; Q8GWW4; 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:UniProtKB.
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:UniProtKB.
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; IPR030519; GUX.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11183:SF44; PTHR11183:SF44; 1.
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..596
FT /note="UDP-glucuronate:xylan alpha-glucuronosyltransferase
FT 2"
FT /id="PRO_0000416734"
FT TRANSMEM 17..37
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT BINDING 395..397
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 395
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 397
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 424..426
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 451..455
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 504..509
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 504
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT SITE 379
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT VAR_SEQ 591..596
FT /note="RSYLIG -> PNINFRMVSAQLEKCLAFDEKGIKVINLAEEMENTL (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042767"
SQ SEQUENCE 596 AA; 70059 MW; A5BDEEF9C7F1588F CRC64;
MTIMTMIMKM APSKSALIRF NLVLLGFSFL LYTAIFFHPS SSVYFSSGAS FVGCSFRDCT
PKVVRGVKMQ ELVEENEINK KDLLTASNQT KLEAPSFMEE ILTRGLGKTK IGMVNMEECD
LTNWKRYGET VHIHFERVSK LFKWQDLFPE WIDEEEETEV PTCPEIPMPD FESLEKLDLV
VVKLPCNYPE EGWRREVLRL QVNLVAANLA AKKGKTDWRW KSKVLFWSKC QPMIEIFRCD
DLEKREADWW LYRPEVVRLQ QRLSLPVGSC NLALPLWAPQ GVDKVYDLTK IEAETKRPKR
EAYVTVLHSS ESYVCGAITL AQSLLQTNTK RDLILLHDDS ISITKLRALA AAGWKLRRII
RIRNPLAEKD SYNEYNYSKF RLWQLTDYDK VIFIDADIIV LRNLDLLFHF PQMSATGNDV
WIYNSGIMVI EPSNCTFTTI MSQRSEIVSY NGGDQGYLNE IFVWWHRLPR RVNFLKNFWS
NTTKERNIKN NLFAAEPPQV YAVHYLGWKP WLCYRDYDCN YDVDEQLVYA SDAAHVRWWK
VHDSMDDALQ KFCRLTKKRR TEINWERRKA RLRGSTDYHW KINVTDPRRR RSYLIG
