GAUTB_ARATH
ID GAUTB_ARATH Reviewed; 537 AA.
AC Q949Q1; A0A178WM53; A0A1W6AJX8; A1A6J4; Q9FZ79;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Hexosyltransferase GAUT11 {ECO:0000305};
DE EC=2.4.1.43 {ECO:0000269|PubMed:30228108};
DE AltName: Full=Galacturonosyltransferase 11 {ECO:0000303|PubMed:16540543};
GN Name=GAUT11 {ECO:0000303|PubMed:16540543};
GN OrderedLocusNames=At1g18580 {ECO:0000312|Araport:AT1G18580};
GN ORFNames=F25I16.8 {ECO:0000312|EMBL:AAF98416.1};
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].
RC STRAIN=cv. Columbia;
RA Zeng W., Gluza P., Heazlewood J.;
RT "Arabidopsis glycosyltransfereases: an update.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-332.
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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 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).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, SUBCELLULAR LOCATION, CATALYTIC
RP ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=30228108; DOI=10.1104/pp.18.00584;
RA Voiniciuc C., Engle K.A., Guenl M., Dieluweit S., Schmidt M.H., Yang J.Y.,
RA Moremen K.W., Mohnen D., Usadel B.;
RT "Identification of key enzymes for pectin synthesis in seed mucilage.";
RL Plant Physiol. 178:1045-1064(2018).
CC -!- FUNCTION: Glycosyltransferase involved in pectin and/or xylans
CC biosynthesis in cell walls (By similarity). Required for the
CC biosynthesis of pectin in seed coat epidermal (SCE) cells
CC (PubMed:30228108). Collaboratively with MUCI70, essential for the
CC accumulation of seed mucilage, a gelatinous wall rich in unbranched
CC rhamnogalacturonan I (RG I), and for shaping the surface morphology of
CC seeds (PubMed:30228108). Catalyzes homogalacturonan (HG) elongation by
CC acting as an HG alpha-1,4 galacturonic acid transferase
CC (PubMed:30228108). {ECO:0000250|UniProtKB:Q9LE59,
CC ECO:0000269|PubMed:30228108}.
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:30228108};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13574;
CC Evidence={ECO:0000269|PubMed:30228108};
CC -!- PATHWAY: Glycan metabolism; pectin biosynthesis.
CC {ECO:0000269|PubMed:30228108}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:30228108}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, inflorescences, siliques,
CC seeds, leaves and stems. {ECO:0000269|PubMed:19825675,
CC ECO:0000269|PubMed:30228108}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in developing seeds in siliques,
CC mainly in the seed coat and, to a lesser extent, in the embryo.
CC {ECO:0000269|PubMed:30228108}.
CC -!- DISRUPTION PHENOTYPE: Strong reduction of seed mucilage accumulation,
CC associated with reduced absolute levels of rhamnose (Rha), galacturonic
CC acid (GalA) and xylose (Xyl) but increased absolute abundance of minor
CC sugars (e.g. galactose (Gal), glucose (Glc) and mannose (Man))
CC (PubMed:30228108). The double mutant muci70-1 gaut11-3 is completely
CC defective in seed mucilage production and exhibits a strong release of
CC minor sugars in total mucilage extracts (PubMed:30228108).
CC {ECO:0000269|PubMed:30228108}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF98416.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABL66770.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; KY906027; ARJ31391.1; -; mRNA.
DR EMBL; AC026238; AAF98416.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29731.1; -; Genomic_DNA.
DR EMBL; AY050967; AAK93644.1; -; mRNA.
DR EMBL; AY062444; AAL32522.1; -; mRNA.
DR EMBL; BT029514; ABL66770.1; ALT_FRAME; mRNA.
DR PIR; D86319; D86319.
DR RefSeq; NP_564057.4; NM_101716.7.
DR AlphaFoldDB; Q949Q1; -.
DR STRING; 3702.AT1G18580.1; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR PaxDb; Q949Q1; -.
DR PRIDE; Q949Q1; -.
DR ProteomicsDB; 224292; -.
DR EnsemblPlants; AT1G18580.1; AT1G18580.1; AT1G18580.
DR GeneID; 838439; -.
DR Gramene; AT1G18580.1; AT1G18580.1; AT1G18580.
DR KEGG; ath:AT1G18580; -.
DR Araport; AT1G18580; -.
DR TAIR; locus:2027453; AT1G18580.
DR eggNOG; ENOG502QRMA; Eukaryota.
DR HOGENOM; CLU_010770_5_0_1; -.
DR InParanoid; Q949Q1; -.
DR OMA; HEDHVEQ; -.
DR OrthoDB; 634904at2759; -.
DR PhylomeDB; Q949Q1; -.
DR UniPathway; UPA00845; -.
DR PRO; PR:Q949Q1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q949Q1; baseline and differential.
DR Genevisible; Q949Q1; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000137; C:Golgi cis 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:0016757; F:glycosyltransferase activity; IDA:TAIR.
DR GO; GO:0047262; F:polygalacturonate 4-alpha-galacturonosyltransferase activity; IDA:TAIR.
DR GO; GO:0052546; P:cell wall pectin metabolic process; IGI:TAIR.
DR GO; GO:0010442; P:guard cell morphogenesis; IGI:TAIR.
DR GO; GO:0010192; P:mucilage biosynthetic process; IMP:TAIR.
DR GO; GO:0080001; P:mucilage extrusion from seed coat; IMP:TAIR.
DR GO; GO:0048358; P:mucilage pectin biosynthetic process; IMP:TAIR.
DR GO; GO:0010246; P:rhamnogalacturonan I 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 wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..537
FT /note="Hexosyltransferase GAUT11"
FT /id="PRO_0000392561"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 17..37
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..537
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 537 AA; 61879 MW; D5D45576C3B145D0 CRC64;
MRRWPVDHRR RGRRRLSSWI WFLLGSFSVA GLVLFIVQHY HHQQDPSQLL LERDTRTEMV
SPPHLNFTEE VTSASSFSRQ LAEQMTLAKA YVFIAKEHNN LHLAWELSSK IRSCQLLLSK
AAMRGQPISF DEAKPIITGL SALIYKAQDA HYDIATTMMT MKSHIQALEE RANAATVQTT
IFGQLVAEAL PKSLHCLTIK LTSDWVTEPS RHELADENRN SPRLVDNNLY HFCIFSDNVI
ATSVVVNSTV SNADHPKQLV FHIVTNRVSY KAMQAWFLSN DFKGSAIEIR SVEEFSWLNA
SYSPVVKQLL DTDARAYYFG EQTSQDTISE PKVRNPKYLS LLNHLRFYIP EIYPQLEKIV
FLDDDVVVQK DLTPLFSLDL HGNVNGAVET CLEAFHRYYK YLNFSNPLIS SKFDPQACGW
AFGMNVFDLI AWRNANVTAR YHYWQDQNRE RTLWKLGTLP PGLLSFYGLT EPLDRRWHVL
GLGYDVNIDN RLIETAAVIH YNGNMKPWLK LAIGRYKPFW LKFLNSSHPY LQDCVTA
