GUX5_ARATH
ID GUX5_ARATH Reviewed; 566 AA.
AC F4HZC3; O04031;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Putative UDP-glucuronate:xylan alpha-glucuronosyltransferase 5;
DE Short=UDP-GlcA:xylan glucuronyltransferase 5;
DE EC=2.4.1.-;
DE AltName: Full=Glycogenin-like protein 5;
DE AltName: Full=Plant glycogenin-like starch initiation protein 5;
DE AltName: Full=Protein GLUCURONIC ACID SUBSTITUTION OF XYLAN 5;
DE Short=AtGUX5;
GN Name=GUX5; Synonyms=PGSIP5; OrderedLocusNames=At1g08990; ORFNames=F7G19.14;
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] OF 59-566.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAB70408.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BX815902; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AC000106; AAB70408.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28380.1; -; Genomic_DNA.
DR EMBL; BX815902; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; G86221; G86221.
DR RefSeq; NP_172373.3; NM_100770.5.
DR AlphaFoldDB; F4HZC3; -.
DR SMR; F4HZC3; -.
DR STRING; 3702.AT1G08990.1; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR PaxDb; F4HZC3; -.
DR PRIDE; F4HZC3; -.
DR ProteomicsDB; 247322; -.
DR EnsemblPlants; AT1G08990.1; AT1G08990.1; AT1G08990.
DR GeneID; 837420; -.
DR Gramene; AT1G08990.1; AT1G08990.1; AT1G08990.
DR KEGG; ath:AT1G08990; -.
DR Araport; AT1G08990; -.
DR TAIR; locus:2036024; AT1G08990.
DR eggNOG; KOG1950; Eukaryota.
DR HOGENOM; CLU_023070_1_0_1; -.
DR InParanoid; F4HZC3; -.
DR OMA; ERIVKWR; -.
DR OrthoDB; 1424146at2759; -.
DR PRO; PR:F4HZC3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HZC3; baseline and differential.
DR Genevisible; F4HZC3; 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: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 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..566
FT /note="Putative UDP-glucuronate:xylan alpha-
FT glucuronosyltransferase 5"
FT /id="PRO_0000416737"
FT TRANSMEM 17..37
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT BINDING 372..374
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 372
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 374
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 401..403
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 428..432
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 475..480
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 475
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT SITE 356
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P13280"
SQ SEQUENCE 566 AA; 65633 MW; 845DA047F730028D CRC64;
MGAKSKSSST RFFMFYLILI SLSFLGLLLN FKPLFLLNPM IASPSIVEIR YSLPEPVKRT
PIWLRLIRNY LPDEKKIRVG LLNIAENERE SYEASGTSIL ENVHVSLDPL PNNLTWTSLF
PVWIDEDHTW HIPSCPEVPL PKMEGSEADV DVVVVKVPCD GFSEKRGLRD VFRLQVNLAA
ANLVVESGRR NVDRTVYVVF IGSCGPMHEI FRCDERVKRV GDYWVYRPDL TRLKQKLLMP
PGSCQIAPLG QGEAWIQDKN RNLTSEKTTL SSFTAQRVAY VTLLHSSEVY VCGAIALAQS
IRQSGSTKDM ILLHDDSITN ISLIGLSLAG WKLRRVERIR SPFSKKRSYN EWNYSKLRVW
QVTDYDKLVF IDADFIIVKN IDYLFSYPQL SAAGNNKVLF NSGVMVLEPS ACLFEDLMLK
SFKIGSYNGG DQGFLNEYFV WWHRLSKRLN TMKYFGDESR HDKARNLPEN LEGIHYLGLK
PWRCYRDYDC NWDLKTRRVY ASESVHARWW KVYDKMPKKL KGYCGLNLKM EKNVEKWRKM
AKLNGFPENH WKIRIKDPRK KNRLSQ
