ID   GAUT9_ARATH             Reviewed;         561 AA.
AC   Q9FWA4;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Probable galacturonosyltransferase 9;
DE            EC=2.4.1.-;
GN   Name=GAUT9; OrderedLocusNames=At3g02350; ORFNames=F11A12.4, F11A12_103;
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=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   [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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [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 synthesis. {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, siliques,
CC       leaves and stems. {ECO:0000269|PubMed:19825675}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
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DR   EMBL; AC068900; AAG12603.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE73795.1; -; Genomic_DNA.
DR   EMBL; AY078957; AAL84957.1; -; mRNA.
DR   EMBL; BT004530; AAO42776.1; -; mRNA.
DR   EMBL; AY084528; AAM61096.1; -; mRNA.
DR   RefSeq; NP_566170.1; NM_111102.2.
DR   AlphaFoldDB; Q9FWA4; -.
DR   STRING; 3702.AT3G02350.1; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   PaxDb; Q9FWA4; -.
DR   PRIDE; Q9FWA4; -.
DR   ProteomicsDB; 222163; -.
DR   EnsemblPlants; AT3G02350.1; AT3G02350.1; AT3G02350.
DR   GeneID; 820474; -.
DR   Gramene; AT3G02350.1; AT3G02350.1; AT3G02350.
DR   KEGG; ath:AT3G02350; -.
DR   Araport; AT3G02350; -.
DR   TAIR; locus:2074572; AT3G02350.
DR   eggNOG; ENOG502QPP9; Eukaryota.
DR   HOGENOM; CLU_010770_5_0_1; -.
DR   InParanoid; Q9FWA4; -.
DR   OMA; TRVDLIH; -.
DR   OrthoDB; 384788at2759; -.
DR   PhylomeDB; Q9FWA4; -.
DR   UniPathway; UPA00845; -.
DR   PRO; PR:Q9FWA4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9FWA4; baseline and differential.
DR   Genevisible; Q9FWA4; 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:0005802; C:trans-Golgi network; HDA:TAIR.
DR   GO; GO:0047262; F:polygalacturonate 4-alpha-galacturonosyltransferase activity; ISS:TAIR.
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   Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..561
FT                   /note="Probable galacturonosyltransferase 9"
FT                   /id="PRO_0000206063"
FT   TOPO_DOM        1..27
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        28..48
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..561
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        346
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        426
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   561 AA;  64160 MW;  47951B05D0B6DE8C CRC64;
     MAVAFRGGRG GVGSGQSTGL RSFFSYRIFI SALFSFLFLA TFSVVLNSSR HQPHQDHTLP
     SMGNAYMQRT FLALQSDPLK TRLDLIHKQA IDHLTLVNAY AAYARKLKLD ASKQLKLFED
     LAINFSDLQS KPGLKSAVSD NGNALEEDSF RQLEKEVKDK VKTARMMIVE SKESYDTQLK
     IQKLKDTIFA VQEQLTKAKK NGAVASLISA KSVPKSLHCL AMRLVGERIS NPEKYKDAPP
     DPAAEDPTLY HYAIFSDNVI AVSVVVRSVV MNAEEPWKHV FHVVTDRMNL AAMKVWFKMR
     PLDRGAHVEI KSVEDFKFLN SSYAPVLRQL ESAKLQKFYF ENQAENATKD SHNLKFKNPK
     YLSMLNHLRF YLPEMYPKLN KILFLDDDVV VQKDVTGLWK INLDGKVNGA VETCFGSFHR
     YGQYLNFSHP LIKENFNPSA CAWAFGMNIF DLNAWRREKC TDQYHYWQNL NEDRTLWKLG
     TLPPGLITFY SKTKSLDKSW HVLGLGYNPG VSMDEIRNAG VIHYNGNMKP WLDIAMNQYK
     SLWTKYVDNE MEFVQMCNFG L