GUX6_ARATH
ID GUX6_ARATH Reviewed; 537 AA.
AC Q8GWB7; Q8W118; W8Q2T0;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Inositol phosphorylceramide glucuronosyltransferase 1 {ECO:0000303|PubMed:25122154};
DE EC=2.4.1.17 {ECO:0000269|PubMed:25122154};
DE AltName: Full=Glycogenin-like protein 6 {ECO:0000303|PubMed:22706449};
DE AltName: Full=Plant glycogenin-like starch initiation protein 6 {ECO:0000303|PubMed:22706449};
GN Name=IPUT1 {ECO:0000303|PubMed:25122154};
GN Synonyms=PGSIP6 {ECO:0000303|PubMed:22706449};
GN OrderedLocusNames=At5g18480 {ECO:0000312|Araport:AT5G18480};
GN ORFNames=T28N17.3 {ECO:0000312|EMBL:AC051626};
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], FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION
RP PHENOTYPE, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=25122154; DOI=10.1105/tpc.114.129171;
RA Rennie E.A., Ebert B., Miles G.P., Cahoon R.E., Christiansen K.M.,
RA Stonebloom S., Khatab H., Twell D., Petzold C.J., Adams P.D., Dupree P.,
RA Heazlewood J.L., Cahoon E.B., Scheller H.V.;
RT "Identification of a sphingolipid alpha-glucuronosyltransferase that is
RT essential for pollen function in Arabidopsis.";
RL Plant Cell 26:3314-3325(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
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 [5]
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 [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=22706449; DOI=10.1104/pp.112.200964;
RA Rennie E.A., Hansen S.F., Baidoo E.E.K., Hadi M.Z., Keasling J.D.,
RA Scheller H.V.;
RT "Three members of the Arabidopsis glycosyltransferase family 8 are xylan
RT glucuronosyltransferases.";
RL Plant Physiol. 159:1408-1417(2012).
RN [8]
RP REVIEW ON SPHINGOLIPIDS.
RX PubMed=23499054; DOI=10.1016/j.pbi.2013.02.009;
RA Markham J.E., Lynch D.V., Napier J.A., Dunn T.M., Cahoon E.B.;
RT "Plant sphingolipids: function follows form.";
RL Curr. Opin. Plant Biol. 16:350-357(2013).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=27643972; DOI=10.1111/tpj.13382;
RA Tartaglio V., Rennie E.A., Cahoon R., Wang G., Baidoo E., Mortimer J.C.,
RA Cahoon E.B., Scheller H.V.;
RT "Glycosylation of inositol phosphorylceramide sphingolipids is required for
RT normal growth and reproduction in Arabidopsis.";
RL Plant J. 89:278-290(2017).
RN [10]
RP REVIEW.
RX PubMed=32407692; DOI=10.1016/j.tplants.2020.03.007;
RA Mortimer J.C., Scheller H.V.;
RT "Synthesis and function of complex sphingolipid glycosylation.";
RL Trends Plant Sci. 25:522-524(2020).
CC -!- FUNCTION: Mediates the transfer of glucuronic acid (GlcA) from UDP-GlcA
CC to glycosyl inositol phosphorylceramides (GIPCs) (PubMed:25122154,
CC PubMed:27643972). The formation of GIPCs sphingolipids is essential for
CC pollen function, plant growth and defense (PubMed:25122154,
CC PubMed:27643972). Required for global fitness (PubMed:27643972).
CC {ECO:0000269|PubMed:25122154, ECO:0000269|PubMed:27643972}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor
CC beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17;
CC Evidence={ECO:0000269|PubMed:25122154};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1D-myo-inositol-1-phospho-N-[(R)-2-hydroxy-very-long-chain
CC fatty acyl]-(R)-4-hydroxysphingoid base + UDP-alpha-D-glucuronate =
CC an alpha-D-glucuronosyl-(1<->6)-1D-myo-inositol-1-phospho-N-[(R)-2-
CC hydroxy-very-long-chain fatty acyl]-(R)-4-hydroxysphingoid base +
CC H(+) + UDP; Xref=Rhea:RHEA:65576, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:155926,
CC ChEBI:CHEBI:156567; Evidence={ECO:0000269|PubMed:25122154,
CC ECO:0000269|PubMed:27643972};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P46976};
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:27643972}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:22706449}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves, stems and
CC siliques. {ECO:0000269|PubMed:25122154}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout pollen development.
CC {ECO:0000269|PubMed:25122154}.
CC -!- DISRUPTION PHENOTYPE: Defect in transmission of mutated alleles through
CC the male gametophyte (e.g. pollen) (PubMed:25122154). Pollen rescued
CC mutants show severe dwarfism with reduced roots, compromised pollen
CC tube guidance, and constitutive activation of salicyclic acid-mediated
CC defense pathways. They have also an altered sphingolipidome with
CC reduced glycosyl inositol phosphorylceramides (GIPCs), increased
CC ceramides, and an increased incorporation of short-chain fatty acids
CC and dihydroxylated bases into inositol phosphorylceramides and GIPCs
CC (PubMed:27643972). {ECO:0000269|PubMed:25122154,
CC ECO:0000269|PubMed:27643972}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin
CC subfamily. {ECO:0000305}.
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DR EMBL; KJ138680; AHL38620.1; -; mRNA.
DR EMBL; AC051626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92569.1; -; Genomic_DNA.
DR EMBL; AK118951; BAC43531.1; -; mRNA.
DR EMBL; AF462795; AAL58891.1; -; mRNA.
DR EMBL; AY143921; AAN28860.1; -; mRNA.
DR RefSeq; NP_197349.2; NM_121853.4.
DR AlphaFoldDB; Q8GWB7; -.
DR SMR; Q8GWB7; -.
DR STRING; 3702.AT5G18480.1; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR SwissPalm; Q8GWB7; -.
DR PaxDb; Q8GWB7; -.
DR PRIDE; Q8GWB7; -.
DR ProteomicsDB; 247275; -.
DR EnsemblPlants; AT5G18480.1; AT5G18480.1; AT5G18480.
DR GeneID; 831966; -.
DR Gramene; AT5G18480.1; AT5G18480.1; AT5G18480.
DR KEGG; ath:AT5G18480; -.
DR Araport; AT5G18480; -.
DR TAIR; locus:2146173; AT5G18480.
DR eggNOG; KOG1950; Eukaryota.
DR HOGENOM; CLU_030312_0_0_1; -.
DR InParanoid; Q8GWB7; -.
DR OMA; CIRSLCA; -.
DR OrthoDB; 1424146at2759; -.
DR PhylomeDB; Q8GWB7; -.
DR BioCyc; ARA:AT5G18480-MON; -.
DR BRENDA; 2.4.1.17; 399.
DR PRO; PR:Q8GWB7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GWB7; baseline and differential.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0005797; C:Golgi medial cisterna; HDA: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:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA: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:1990482; F:sphingolipid alpha-glucuronosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046513; P:ceramide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006673; P:inositol phosphoceramide metabolic process; IDA:UniProtKB.
DR GO; GO:0009555; P:pollen development; IMP:UniProtKB.
DR GO; GO:0010183; P:pollen tube guidance; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Glycosyltransferase; Golgi apparatus; Manganese; Membrane; Metal-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..537
FT /note="Inositol phosphorylceramide glucuronosyltransferase
FT 1"
FT /id="PRO_0000416738"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 124..126
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 124
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT BINDING 126
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT BINDING 153..155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 180..184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 248..255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT SITE 108
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT CONFLICT 182
FT /note="G -> R (in Ref. 5; AAL58891/AAN28860)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="G -> E (in Ref. 5; AAL58891/AAN28860)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 60011 MW; AA561C73A1064E2F CRC64;
MVRLKTSLWV LLLALVSIQL NGSFGSESSK VAYVTLLYGD EFLLGVRVLG KSIRDTGSTK
DMVALVSDGV SDYSKKLLKA DGWKVEKISL LANPNQVHPT RFWGVYTKLK IFNMTDYKKV
VYLDADTIVV KNIEDLFKCS KFCANLKHSE RLNSGVMVVE PSEALFNDMM RKVKTLSSYT
GGDQGFLNSY YPDFPNARVF DPSVTPEVLK TRPVPAMERL STLYNADVGL YMLANKWMVD
DSKLHVIHYT LGPLKPWDWW TAWLVKPVDA WHSIRVKLEE TLPGTGGGSN QHDELVVKFL
FLLPLCALLF CIYRSIQGRE GSLCWSSFSN QIRYLYYKVR SNGTLGYGGV STMSPSYQPH
SGNAQSKVPQ HLGAVSVVVC FTAVLLSLGI SFAIVPRQIM PWTGLVLVYE WTFTIFFLLF
GVFLLFVHQH GKRIAIQSES SSLDDSAKVH QRAGGSCDVT TLYYGLGMAF LAIAAVSLPY
ILGITALFTR LGLMVGLAII LAAFMTYASE HLAVRWFLKG LEDRRDTTRS NSLCFLC
