GAUT6_ARATH
ID GAUT6_ARATH Reviewed; 589 AA.
AC Q9M9Y5;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Probable galacturonosyltransferase 6;
DE EC=2.4.1.-;
GN Name=GAUT6; OrderedLocusNames=At1g06780; ORFNames=F4H5.13;
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=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 [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=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 [5]
RP FUNCTION, 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: Probably involved in pectin biosynthesis in cell walls.
CC {ECO:0000269|PubMed:19825675}.
CC -!- PATHWAY: Glycan metabolism; pectin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II
CC membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9M9Y5-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, inflorescences, siliques,
CC leaves and stems. {ECO:0000269|PubMed:19825675}.
CC -!- DISRUPTION PHENOTYPE: Reduced galacturonic acid content in cell wall.
CC {ECO:0000269|PubMed:19825675}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
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DR EMBL; AC011001; AAF63140.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28035.1; -; Genomic_DNA.
DR EMBL; AY045900; AAK76574.1; -; mRNA.
DR EMBL; AY091452; AAM14391.1; -; mRNA.
DR PIR; F86202; F86202.
DR RefSeq; NP_563771.1; NM_100555.3. [Q9M9Y5-1]
DR AlphaFoldDB; Q9M9Y5; -.
DR SMR; Q9M9Y5; -.
DR STRING; 3702.AT1G06780.2; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR PaxDb; Q9M9Y5; -.
DR PRIDE; Q9M9Y5; -.
DR ProteomicsDB; 224291; -. [Q9M9Y5-1]
DR EnsemblPlants; AT1G06780.1; AT1G06780.1; AT1G06780. [Q9M9Y5-1]
DR GeneID; 837189; -.
DR Gramene; AT1G06780.1; AT1G06780.1; AT1G06780. [Q9M9Y5-1]
DR KEGG; ath:AT1G06780; -.
DR Araport; AT1G06780; -.
DR eggNOG; ENOG502QT8Z; Eukaryota.
DR HOGENOM; CLU_010770_2_1_1; -.
DR InParanoid; Q9M9Y5; -.
DR OMA; EPSFHSM; -.
DR PhylomeDB; Q9M9Y5; -.
DR UniPathway; UPA00845; -.
DR PRO; PR:Q9M9Y5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M9Y5; baseline and differential.
DR Genevisible; Q9M9Y5; AT.
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:0047262; F:polygalacturonate 4-alpha-galacturonosyltransferase activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..589
FT /note="Probable galacturonosyltransferase 6"
FT /id="PRO_0000392559"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..589
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 127..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 589 AA; 67537 MW; 02B583F503E4C205 CRC64;
MKQIRRWQRI LILALLSISV FAPLIFVSNR LKSITPVGRR EFIEELSKIR FTTNDLRLSA
IEHEDGEGLK GPRLILFKDG EFNSSAESDG GNTYKNREEQ VIVSQKMTVS SDEKGQILPT
VNQLANKTDF KPPLSKGEKN TRVQPDRATD VKTKEIRDKI IQAKAYLNFA PPGSNSQVVK
ELRGRLKELE RSVGDATKDK DLSKGALRRV KPMENVLYKA SRVFNNCPAI ATKLRAMNYN
TEEQVQAQKN QAAYLMQLAA RTTPKGLHCL SMRLTSEYFS LDPEKRQMPN QQNYFDANFN
HYVVFSDNVL ASSVVVNSTI SSSKEPERIV FHVVTDSLNY PAISMWFLLN IQSKATIQIL
NIDDMDVLPR DYDQLLMKQN SNDPRFISTL NHARFYLPDI FPGLNKMVLL DHDVVVQRDL
SRLWSIDMKG KVVGAVETCL EGESSFRSMS TFINFSDTWV AGKFSPRACT WAFGMNLIDL
EEWRIRKLTS TYIKYFNLGT KRPLWKAGSL PIGWLTFYRQ TLALDKRWHV MGLGRESGVK
AVDIEQAAVI HYDGVMKPWL DIGKENYKRY WNIHVPYHHT YLQQCNLQA
