GAUT7_ARATH
ID GAUT7_ARATH Reviewed; 619 AA.
AC Q9ZVI7; Q949N9;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Probable galacturonosyltransferase 7;
DE EC=2.4.1.-;
DE AltName: Full=Like glycosyl transferase 7;
GN Name=GAUT7; Synonyms=JS33, LGT7; OrderedLocusNames=At2g38650;
GN ORFNames=T6A23.15;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 GENE FAMILY, AND NOMENCLATURE.
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 [5]
RP IDENTIFICATION BY 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 [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: May be involved in pectin biosynthesis. {ECO:0000250}.
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 roots, inflorescences, flowers,
CC siliques, leaves and stems. {ECO:0000269|PubMed:16540543,
CC ECO:0000269|PubMed:19825675}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC005499; AAC67353.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09562.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09563.1; -; Genomic_DNA.
DR EMBL; AY050982; AAK93659.1; -; mRNA.
DR EMBL; AY091448; AAM14387.1; -; mRNA.
DR PIR; F84807; F84807.
DR RefSeq; NP_001189702.1; NM_001202773.2.
DR RefSeq; NP_565893.1; NM_129422.4.
DR AlphaFoldDB; Q9ZVI7; -.
DR SMR; Q9ZVI7; -.
DR BioGRID; 3789; 14.
DR STRING; 3702.AT2G38650.2; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR iPTMnet; Q9ZVI7; -.
DR PaxDb; Q9ZVI7; -.
DR PRIDE; Q9ZVI7; -.
DR ProteomicsDB; 222162; -.
DR EnsemblPlants; AT2G38650.1; AT2G38650.1; AT2G38650.
DR EnsemblPlants; AT2G38650.2; AT2G38650.2; AT2G38650.
DR GeneID; 818447; -.
DR Gramene; AT2G38650.1; AT2G38650.1; AT2G38650.
DR Gramene; AT2G38650.2; AT2G38650.2; AT2G38650.
DR KEGG; ath:AT2G38650; -.
DR Araport; AT2G38650; -.
DR TAIR; locus:2064163; AT2G38650.
DR eggNOG; ENOG502QVSX; Eukaryota.
DR HOGENOM; CLU_010770_4_0_1; -.
DR InParanoid; Q9ZVI7; -.
DR OMA; NGAVKFC; -.
DR OrthoDB; 788190at2759; -.
DR PhylomeDB; Q9ZVI7; -.
DR BRENDA; 2.4.1.43; 399.
DR UniPathway; UPA00845; -.
DR PRO; PR:Q9ZVI7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZVI7; baseline and differential.
DR Genevisible; Q9ZVI7; AT.
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:0047262; F:polygalacturonate 4-alpha-galacturonosyltransferase activity; ISS:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045489; P:pectin biosynthetic process; IEA:UniProtKB-UniPathway.
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..619
FT /note="Probable galacturonosyltransferase 7"
FT /id="PRO_0000392299"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..619
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 95..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 619 AA; 69749 MW; B7DC511222D36C94 CRC64;
MKGGGGGGGG GGGGKRRWKV LVIGVLVLVI LSMLVPLAFL LGLHNGFHSP GFVTVQPASS
FESFTRINAT KHTQRDVSER VDEVLQKINP VLPKKSDINV GSRDVNATSG TDSKKRGLPV
SPTVVANPSP ANKTKSEASY TGVQRKIVSG DETWRTCEVK YGSYCLWREE NKEPMKDAKV
KQMKDQLFVA RAYYPSIAKM PSQSKLTRDM KQNIQEFERI LSESSQDADL PPQVDKKLQK
MEAVIAKAKS FPVDCNNVDK KLRQILDLTE DEASFHMKQS VFLYQLAVQT MPKSLHCLSM
RLTVEHFKSD SLEDPISEKF SDPSLLHFVI ISDNILASSV VINSTVVHAR DSKNFVFHVL
TDEQNYFAMK QWFIRNPCKQ STVQVLNIEK LELDDSDMKL SLSAEFRVSF PSGDLLASQQ
NRTHYLSLFS QSHYLLPKLF DKLEKVVILD DDVVVQRDLS PLWDLDMEGK VNGAVKSCTV
RLGQLRSLKR GNFDTNACLW MSGLNVVDLA RWRALGVSET YQKYYKEMSS GDESSEAIAL
QASLLTFQDQ VYALDDKWAL SGLGYDYYIN AQAIKNAAIL HYNGNMKPWL ELGIPNYKNY
WRRHLSREDR FLSDCNVNP
