GUX4_ARATH
ID GUX4_ARATH Reviewed; 557 AA.
AC Q9FZ37;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Putative UDP-glucuronate:xylan alpha-glucuronosyltransferase 4;
DE Short=UDP-GlcA:xylan glucuronyltransferase 4;
DE EC=2.4.1.-;
DE AltName: Full=Glycogenin-like protein 4;
DE AltName: Full=Plant glycogenin-like starch initiation protein 4;
DE AltName: Full=Protein GLUCURONIC ACID SUBSTITUTION OF XYLAN 4;
DE Short=AtGUX4;
GN Name=GUX4; Synonyms=PGSIP4; OrderedLocusNames=At1g54940;
GN ORFNames=F14C21.47, T24C10.6;
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 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).
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 {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin
CC subfamily. {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; AC064840; AAG00875.1; -; Genomic_DNA.
DR EMBL; AC069144; AAG51129.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33165.1; -; Genomic_DNA.
DR PIR; H96590; H96590.
DR RefSeq; NP_175891.1; NM_104367.2.
DR AlphaFoldDB; Q9FZ37; -.
DR SMR; Q9FZ37; -.
DR STRING; 3702.AT1G54940.1; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR PaxDb; Q9FZ37; -.
DR PRIDE; Q9FZ37; -.
DR ProteomicsDB; 247321; -.
DR EnsemblPlants; AT1G54940.1; AT1G54940.1; AT1G54940.
DR GeneID; 841934; -.
DR Gramene; AT1G54940.1; AT1G54940.1; AT1G54940.
DR KEGG; ath:AT1G54940; -.
DR Araport; AT1G54940; -.
DR TAIR; locus:2011045; AT1G54940.
DR eggNOG; KOG1950; Eukaryota.
DR HOGENOM; CLU_023070_1_0_1; -.
DR InParanoid; Q9FZ37; -.
DR OMA; NGPSIME; -.
DR OrthoDB; 1424146at2759; -.
DR PhylomeDB; Q9FZ37; -.
DR PRO; PR:Q9FZ37; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZ37; baseline and differential.
DR Genevisible; Q9FZ37; 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: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:0045492; P:xylan biosynthetic process; IBA:GO_Central.
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 3: Inferred from homology;
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..557
FT /note="Putative UDP-glucuronate:xylan alpha-
FT glucuronosyltransferase 4"
FT /id="PRO_0000416736"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT BINDING 365..367
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 365
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 367
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 394..396
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 421..425
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 466..471
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 466
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT SITE 349
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P13280"
SQ SEQUENCE 557 AA; 64709 MW; 4545CCDA3ED14E1F CRC64;
MGTKTHNSRG KIFMIYLILV SLSLLGLILP FKPLFRITSP SSTLRIDLPS PQVNKNPKWL
RLIRNYLPEK RIQVGFLNID EKERESYEAR GPLVLKNIHV PLDHIPKNVT WKSLYPEWIN
EEASTCPEIP LPQPEGSDAN VDVIVARVPC DGWSANKGLR DVFRLQVNLA AANLAVQSGL
RTVNQAVYVV FIGSCGPMHE IFPCDERVMR VEDYWVYKPY LPRLKQKLLM PVGSCQIAPS
FAQFGQEAWR PKHEDNLASK AVTALPRRLR VAYVTVLHSS EAYVCGAIAL AQSIRQSGSH
KDMILLHDHT ITNKSLIGLS AAGWNLRLID RIRSPFSQKD SYNEWNYSKL RVWQVTDYDK
LVFIDADFII LKKLDHLFYY PQLSASGNDK VLFNSGIMVL EPSACMFKDL MEKSFKIESY
NGGDQGFLNE IFVWWHRLSK RVNTMKYFDE KNHRRHDLPE NVEGLHYLGL KPWVCYRDYD
CNWDISERRV FASDSVHEKW WKVYDKMSEQ LKGYCGLNKN MEKRIEKWRR IAKNNSLPDR
HWEIEVRDPR KTNLLVQ
