GAUTF_ARATH
ID GAUTF_ARATH Reviewed; 540 AA.
AC Q8L4B0; Q56WW9; Q9LXS3;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Probable galacturonosyltransferase 15;
DE EC=2.4.1.-;
GN Name=GAUT15; OrderedLocusNames=At3g58790; ORFNames=T20N10.140;
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] OF 260-540.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) 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, 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: May be involved in pectin and/or xylans biosynthesis in cell
CC walls. {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 -!- DISRUPTION PHENOTYPE: No changes in the cell wall content.
CC {ECO:0000269|PubMed:19825675}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB88296.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL353032; CAB88296.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79832.1; -; Genomic_DNA.
DR EMBL; AY099698; AAM20549.1; -; mRNA.
DR EMBL; AY128894; AAM91294.1; -; mRNA.
DR EMBL; AK221910; BAD94300.1; -; mRNA.
DR PIR; T49162; T49162.
DR RefSeq; NP_191438.2; NM_115741.3.
DR AlphaFoldDB; Q8L4B0; -.
DR STRING; 3702.AT3G58790.1; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR PaxDb; Q8L4B0; -.
DR PRIDE; Q8L4B0; -.
DR ProteomicsDB; 222165; -.
DR EnsemblPlants; AT3G58790.1; AT3G58790.1; AT3G58790.
DR GeneID; 825048; -.
DR Gramene; AT3G58790.1; AT3G58790.1; AT3G58790.
DR KEGG; ath:AT3G58790; -.
DR Araport; AT3G58790; -.
DR TAIR; locus:2099049; AT3G58790.
DR eggNOG; ENOG502QVXA; Eukaryota.
DR HOGENOM; CLU_010770_5_1_1; -.
DR InParanoid; Q8L4B0; -.
DR OMA; YLHVTIV; -.
DR OrthoDB; 1520602at2759; -.
DR PhylomeDB; Q8L4B0; -.
DR UniPathway; UPA00845; -.
DR PRO; PR:Q8L4B0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8L4B0; baseline and differential.
DR Genevisible; Q8L4B0; 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; 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 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..540
FT /note="Probable galacturonosyltransferase 15"
FT /id="PRO_0000392565"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..540
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 290
FT /note="K -> E (in Ref. 4; BAD94300)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 60620 MW; 99BDDD0A268B6D09 CRC64;
MKFYISATGI KKVTISNPGV GIGKGSGGCA AAAAALAARR FSSRTLLLLL LLLAIVLPFI
FVRFAFLVLE SASVCDSPLD CMGLRLFRGG DTSLKIGEEL TRALVEETTD HQDVNGRGTK
GSLESFDDLV KEMTLKRRDI RAFASVTKKM LLQMERKVQS AKHHELVYWH LASHGIPKSL
HCLSLRLTEE YSVNAMARMR LPPPESVSRL TDPSFHHIVL LTDNVLAASV VISSTVQNAV
NPEKFVFHIV TDKKTYTPMH AWFAINSASS PVVEVKGLHQ YDWPQEVNFK VREMLDIHRL
IWRRHYQNLK DSDFSFVEGT HEQSLQALNP SCLALLNHLR IYIPKLFPDL NKIVLLDDDV
VVQSDLSSLW ETDLNGKVVG AVVDSWCGDN CCPGRKYKDY FNFSHPLISS NLVQEDCAWL
SGMNVFDLKA WRQTNITEAY STWLRLSVRS GLQLWQPGAL PPTLLAFKGL TQSLEPSWHV
AGLGSRSVKS PQEILKSASV LHFSGPAKPW LEISNPEVRS LWYRYVNSSD IFVRKCKIMN
