GUX3_ARATH
ID GUX3_ARATH Reviewed; 618 AA.
AC Q8W4A7; O80649;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Putative UDP-glucuronate:xylan alpha-glucuronosyltransferase 3;
DE Short=UDP-GlcA:xylan glucuronyltransferase 3;
DE EC=2.4.1.-;
DE AltName: Full=Glycogenin-like protein 3;
DE AltName: Full=Plant glycogenin-like starch initiation protein 2;
DE AltName: Full=Protein GLUCURONIC ACID SUBSTITUTION OF XYLAN 3;
DE Short=AtGUX3;
GN Name=GUX3; Synonyms=PGSIP2; OrderedLocusNames=At1g77130; ORFNames=T14N5.1;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
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 [4]
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 [5]
RP SUBCELLULAR LOCATION.
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: May be involved in the substitutions of the xylan backbone in
CC stem glucuronoxylan. {ECO:0000250}.
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}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:20852069}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC34345.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004260; AAC34345.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35939.1; -; Genomic_DNA.
DR EMBL; AY062695; AAL32773.1; -; mRNA.
DR EMBL; AY114677; AAM47996.1; -; mRNA.
DR PIR; T00444; T00444.
DR RefSeq; NP_177838.2; NM_106363.5.
DR AlphaFoldDB; Q8W4A7; -.
DR SMR; Q8W4A7; -.
DR BioGRID; 29268; 1.
DR IntAct; Q8W4A7; 1.
DR STRING; 3702.AT1G77130.1; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR iPTMnet; Q8W4A7; -.
DR PaxDb; Q8W4A7; -.
DR PRIDE; Q8W4A7; -.
DR ProteomicsDB; 247155; -.
DR EnsemblPlants; AT1G77130.1; AT1G77130.1; AT1G77130.
DR GeneID; 844049; -.
DR Gramene; AT1G77130.1; AT1G77130.1; AT1G77130.
DR KEGG; ath:AT1G77130; -.
DR Araport; AT1G77130; -.
DR TAIR; locus:2196020; AT1G77130.
DR eggNOG; KOG1950; Eukaryota.
DR HOGENOM; CLU_023070_1_0_1; -.
DR InParanoid; Q8W4A7; -.
DR OMA; WTDNSTV; -.
DR OrthoDB; 1424146at2759; -.
DR PhylomeDB; Q8W4A7; -.
DR PRO; PR:Q8W4A7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8W4A7; baseline and differential.
DR Genevisible; Q8W4A7; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
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:0015020; F:glucuronosyltransferase activity; IDA: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: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:SF56; PTHR11183:SF56; 1.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Golgi apparatus;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..618
FT /note="Putative UDP-glucuronate:xylan alpha-
FT glucuronosyltransferase 3"
FT /id="PRO_0000416735"
FT TRANSMEM 32..54
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT REGION 598..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 379..381
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 379
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 381
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 408..410
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 435..439
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 489..495
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 489
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT SITE 363
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P13280"
SQ SEQUENCE 618 AA; 71487 MW; F4883619D95D26B6 CRC64;
MIPSSSPMES RHRLSFSNEK TSRRRFQRIE KGVKFNTLKL VLICIMLGAL FTIYRFRYPP
LQIPEIPTSF GLTTDPRYVA TAEINWNHMS NLVEKHVFGR SEYQGIGLIN LNDNEIDRFK
EVTKSDCDHV ALHLDYAAKN ITWESLYPEW IDEVEEFEVP TCPSLPLIQI PGKPRIDLVI
AKLPCDKSGK WSRDVARLHL QLAAARVAAS SKGLHNVHVI LVSDCFPIPN LFTGQELVAR
QGNIWLYKPN LHQLRQKLQL PVGSCELSVP LQAKDNFYSA GAKKEAYATI LHSAQFYVCG
AIAAAQSIRM SGSTRDLVIL VDETISEYHK SGLVAAGWKI QMFQRIRNPN AVPNAYNEWN
YSKFRLWQLT EYSKIIFIDA DMLILRNIDF LFEFPEISAT GNNATLFNSG LMVVEPSNST
FQLLMDNINE VVSYNGGDQG YLNEIFTWWH RIPKHMNFLK HFWEGDEPEI KKMKTSLFGA
DPPILYVLHY LGYNKPWLCF RDYDCNWNVD IFQEFASDEA HKTWWRVHDA MPENLHKFCL
LRSKQKAQLE WDRRQAEKGN YKDGHWKIKI KDKRLKTCFE DFCFWESMLW HWGETNSTNN
SSTTTTSSPP HKTALPSL
