GAUT8_ARATH
ID GAUT8_ARATH Reviewed; 559 AA.
AC Q9LSG3;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Galacturonosyltransferase 8;
DE EC=2.4.1.-;
DE AltName: Full=Glycosyltransferase QUASIMODO1;
GN Name=GAUT8; Synonyms=QUA1; OrderedLocusNames=At3g25140; ORFNames=MJL12.8;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 CHARACTERIZATION.
RX PubMed=12368506; DOI=10.1105/tpc.004259;
RA Bouton S., Leboeuf E., Mouille G., Leydecker M.-T., Talbotec J.,
RA Granier F., Lahaye M., Hoefte H., Truong H.-N.;
RT "QUASIMODO1 encodes a putative membrane-bound glycosyltransferase required
RT for normal pectin synthesis and cell adhesion in Arabidopsis.";
RL Plant Cell 14:2577-2590(2002).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16059719; DOI=10.1007/s00425-005-0008-z;
RA Orfila C., Sorensen S.O., Harholt J., Geshi N., Crombie H., Truong H.N.,
RA Reid J.S., Knox J.P., Scheller H.V.;
RT "QUASIMODO1 is expressed in vascular tissue of Arabidopsis thaliana
RT inflorescence stems, and affects homogalacturonan and xylan biosynthesis.";
RL Planta 222:613-622(2005).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16540543; DOI=10.1073/pnas.0600120103;
RA Sterling J.D., Atmodjo M.A., Inwood S.E., Kumar Kolli V.S., Quigley H.F.,
RA Hahn M.G., Mohnen D.;
RT "Functional identification of an Arabidopsis pectin biosynthetic
RT homogalacturonan galacturonosyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5236-5241(2006).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=17996933; DOI=10.1016/j.ijbiomac.2007.09.020;
RA Rondeau-Mouro C., Defer D., Leboeuf E., Lahaye M.;
RT "Assessment of cell wall porosity in Arabidopsis thaliana by NMR
RT spectroscopy.";
RL Int. J. Biol. Macromol. 42:83-92(2008).
RN [8]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19825675; DOI=10.1093/mp/ssp062;
RA Caffall K.H., Pattathil S., Phillips S.E., Hahn M.G., Mohnen D.;
RT "Arabidopsis thaliana T-DNA mutants implicate GAUT genes in the
RT biosynthesis of pectin and xylan in cell walls and seed testa.";
RL Mol. Plant 2:1000-1014(2009).
CC -!- FUNCTION: Alpha-1-4-D-galacturonosyltransferase involved in
CC homogalacturonan (HGA) synthesis, a class of pectin which plays a role
CC in cell adhesion. {ECO:0000269|PubMed:16059719}.
CC -!- PATHWAY: Glycan metabolism; pectin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, inflorescences, flowers,
CC siliques, leaves and stems. Localized to discrete cells of the vascular
CC tissue and subepidermal layers. {ECO:0000269|PubMed:16059719,
CC ECO:0000269|PubMed:19825675}.
CC -!- DEVELOPMENTAL STAGE: Expressed at both the vegetative and floral
CC stages.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality. Reduced galacturonic acid and
CC xylose content in cell wall. Altered cell wall porosity. Reduced
CC vascular bundle. {ECO:0000269|PubMed:16059719,
CC ECO:0000269|PubMed:17996933, ECO:0000269|PubMed:19825675}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
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DR EMBL; AB026647; BAB02072.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76983.1; -; Genomic_DNA.
DR EMBL; AY099574; AAM20426.1; -; mRNA.
DR EMBL; BT010393; AAQ56836.1; -; mRNA.
DR RefSeq; NP_189150.1; NM_113418.5.
DR AlphaFoldDB; Q9LSG3; -.
DR SMR; Q9LSG3; -.
DR BioGRID; 7436; 1.
DR IntAct; Q9LSG3; 1.
DR STRING; 3702.AT3G25140.1; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR PaxDb; Q9LSG3; -.
DR PRIDE; Q9LSG3; -.
DR ProteomicsDB; 221905; -.
DR EnsemblPlants; AT3G25140.1; AT3G25140.1; AT3G25140.
DR GeneID; 822105; -.
DR Gramene; AT3G25140.1; AT3G25140.1; AT3G25140.
DR KEGG; ath:AT3G25140; -.
DR Araport; AT3G25140; -.
DR TAIR; locus:2090210; AT3G25140.
DR eggNOG; ENOG502QS2Q; Eukaryota.
DR HOGENOM; CLU_010770_5_0_1; -.
DR InParanoid; Q9LSG3; -.
DR OMA; IFTDQAR; -.
DR OrthoDB; 384788at2759; -.
DR PhylomeDB; Q9LSG3; -.
DR BioCyc; ARA:AT3G25140-MON; -.
DR BioCyc; MetaCyc:MON-2483; -.
DR UniPathway; UPA00845; -.
DR PRO; PR:Q9LSG3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSG3; baseline and differential.
DR Genevisible; Q9LSG3; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
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:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0016757; F:glycosyltransferase activity; ISS:TAIR.
DR GO; GO:0047262; F:polygalacturonate 4-alpha-galacturonosyltransferase activity; ISS:TAIR.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0010289; P:homogalacturonan biosynthetic process; IMP:TAIR.
DR GO; GO:0045489; P:pectin biosynthetic process; IMP:TAIR.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029993; GAUT.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR32116; PTHR32116; 1.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..559
FT /note="Galacturonosyltransferase 8"
FT /id="PRO_0000206062"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..559
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 559 AA; 64368 MW; 183A13600FEB40DE CRC64;
MANHHRLLRG GGSPAIIGGR ITLTAFASTI ALFLFTLSFF FASDSNDSPD LLLPGVEYSN
GVGSRRSMLD IKSDPLKPRL IQIRKQADDH RSLALAYASY ARKLKLENSK LVRIFADLSR
NYTDLINKPT YRALYDSDGA SIEESVLRQF EKEVKERIKM TRQVIAEAKE SFDNQLKIQK
LKDTIFAVNE QLTNAKKQGA FSSLIAAKSI PKGLHCLAMR LMEERIAHPE KYTDEGKDRP
RELEDPNLYH YAIFSDNVIA ASVVVNSAVK NAKEPWKHVF HVVTDKMNLG AMQVMFKLKE
YKGAHVEVKA VEDYTFLNSS YVPVLKQLES ANLQKFYFEN KLENATKDTT NMKFRNPKYL
SILNHLRFYL PEMYPKLHRI LFLDDDVVVQ KDLTGLWEID MDGKVNGAVE TCFGSFHRYA
QYMNFSHPLI KEKFNPKACA WAYGMNFFDL DAWRREKCTE EYHYWQNLNE NRALWKLGTL
PPGLITFYST TKPLDKSWHV LGLGYNPSIS MDEIRNAAVV HFNGNMKPWL DIAMNQFRPL
WTKHVDYDLE FVQACNFGL
