GAUT1_ARATH
ID GAUT1_ARATH Reviewed; 673 AA.
AC Q9LE59; Q94BZ8;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Polygalacturonate 4-alpha-galacturonosyltransferase;
DE EC=2.4.1.43;
DE AltName: Full=Alpha-1,4-galacturonosyltransferase 1;
DE AltName: Full=Galacturonosyltransferase 1;
DE AltName: Full=Like glycosyl transferase 1;
GN Name=GAUT1; Synonyms=JS36, LGT1; OrderedLocusNames=At3g61130;
GN ORFNames=T20K12.30;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=10809443; DOI=10.1023/a:1006368316413;
RA Tavares R., Aubourg S., Lecharny A., Kreis M.;
RT "Organization and structural evolution of four multigene families in
RT Arabidopsis thaliana: AtLCAD, AtLGT, AtMYST and AtHD-GL2.";
RL Plant Mol. Biol. 42:703-717(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [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 TISSUE SPECIFICITY.
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: Involved in pectin biosynthesis. Catalyzes the transfer of
CC galacturonic acid from uridine 5'-diphosphogalacturonic acid onto the
CC pectic polysaccharide homogalacturonan. {ECO:0000269|PubMed:16540543}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-galacturonosyl](n) + UDP-alpha-D-galacturonate
CC = [(1->4)-alpha-D-galacturonosyl](n+1) + H(+) + UDP;
CC Xref=Rhea:RHEA:13573, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14571,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57635, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:140523; EC=2.4.1.43;
CC Evidence={ECO:0000269|PubMed:16540543};
CC -!- PATHWAY: Glycan metabolism; pectin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, inflorescences, flowers,
CC siliques, pollen, roots, stems and leaves.
CC {ECO:0000269|PubMed:10809443, ECO:0000269|PubMed:16540543,
CC ECO:0000269|PubMed:19825675}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK62572.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAN18196.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ243015; CAB91508.1; -; Genomic_DNA.
DR EMBL; DQ370437; ABD14404.1; -; mRNA.
DR EMBL; AL137898; CAB71043.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80159.1; -; Genomic_DNA.
DR EMBL; AY039515; AAK62572.1; ALT_FRAME; mRNA.
DR EMBL; BT000630; AAN18196.1; ALT_FRAME; mRNA.
DR PIR; T47905; T47905.
DR RefSeq; NP_191672.1; NM_115977.4.
DR AlphaFoldDB; Q9LE59; -.
DR SMR; Q9LE59; -.
DR BioGRID; 10599; 14.
DR STRING; 3702.AT3G61130.1; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR iPTMnet; Q9LE59; -.
DR PaxDb; Q9LE59; -.
DR PRIDE; Q9LE59; -.
DR ProteomicsDB; 221902; -.
DR EnsemblPlants; AT3G61130.1; AT3G61130.1; AT3G61130.
DR GeneID; 825285; -.
DR Gramene; AT3G61130.1; AT3G61130.1; AT3G61130.
DR KEGG; ath:AT3G61130; -.
DR Araport; AT3G61130; -.
DR TAIR; locus:2098836; AT3G61130.
DR eggNOG; ENOG502QSDQ; Eukaryota.
DR HOGENOM; CLU_010770_2_0_1; -.
DR InParanoid; Q9LE59; -.
DR OMA; ETPTKIH; -.
DR OrthoDB; 409816at2759; -.
DR PhylomeDB; Q9LE59; -.
DR BRENDA; 2.4.1.43; 399.
DR UniPathway; UPA00845; -.
DR PRO; PR:Q9LE59; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LE59; baseline and differential.
DR Genevisible; Q9LE59; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA: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:0047262; F:polygalacturonate 4-alpha-galacturonosyltransferase activity; IDA:TAIR.
DR GO; GO:0010289; P:homogalacturonan biosynthetic process; IDA: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 wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..673
FT /note="Polygalacturonate 4-alpha-galacturonosyltransferase"
FT /id="PRO_0000392298"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..673
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 112..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 673 AA; 77373 MW; 183D507DC4504166 CRC64;
MALKRGLSGV NRIRGSGGGS RSVLVLLIFF CVFAPLCFFV GRGVYIDSSN DYSIVSVKQN
LDWRERLAMQ SVRSLFSKEI LDVIATSTAD LGPLSLDSFK KNNLSASWRG TGVDPSFRHS
ENPATPDVKS NNLNEKRDSI SKDSIHQKVE TPTKIHRRQL REKRREMRAN ELVQHNDDTI
LKLENAAIER SKSVDSAVLG KYSIWRRENE NDNSDSNIRL MRDQVIMARV YSGIAKLKNK
NDLLQELQAR LKDSQRVLGE ATSDADLPRS AHEKLRAMGQ VLAKAKMQLY DCKLVTGKLR
AMLQTADEQV RSLKKQSTFL AQLAAKTIPN PIHCLSMRLT IDYYLLSPEK RKFPRSENLE
NPNLYHYALF SDNVLAASVV VNSTIMNAKD PSKHVFHLVT DKLNFGAMNM WFLLNPPGKA
TIHVENVDEF KWLNSSYCPV LRQLESAAMR EYYFKADHPT SGSSNLKYRN PKYLSMLNHL
RFYLPEVYPK LNKILFLDDD IIVQKDLTPL WEVNLNGKVN GAVETCGESF HRFDKYLNFS
NPHIARNFNP NACGWAYGMN MFDLKEWKKR DITGIYHKWQ NMNENRTLWK LGTLPPGLIT
FYGLTHPLNK AWHVLGLGYN PSIDKKDIEN AAVVHYNGNM KPWLELAMSK YRPYWTKYIK
FDHPYLRRCN LHE
