GAUT5_ARATH
ID GAUT5_ARATH Reviewed; 610 AA.
AC Q8RXE1;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable galacturonosyltransferase 5;
DE EC=2.4.1.-;
DE AltName: Full=Like glycosyl transferase 5;
GN Name=GAUT5; Synonyms=LGT5; OrderedLocusNames=At2g30575; ORFNames=T6B20;
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 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}.
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DR EMBL; U93215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; AEC08410.1; -; Genomic_DNA.
DR EMBL; AY081313; AAL91202.1; -; mRNA.
DR EMBL; BT002563; AAO00923.1; -; mRNA.
DR RefSeq; NP_850150.1; NM_179819.2.
DR AlphaFoldDB; Q8RXE1; -.
DR SMR; Q8RXE1; -.
DR STRING; 3702.AT2G30575.1; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR PaxDb; Q8RXE1; -.
DR PRIDE; Q8RXE1; -.
DR ProteomicsDB; 221904; -.
DR EnsemblPlants; AT2G30575.1; AT2G30575.1; AT2G30575.
DR GeneID; 817607; -.
DR Gramene; AT2G30575.1; AT2G30575.1; AT2G30575.
DR KEGG; ath:AT2G30575; -.
DR Araport; AT2G30575; -.
DR TAIR; locus:504955915; AT2G30575.
DR eggNOG; ENOG502QT8Z; Eukaryota.
DR HOGENOM; CLU_010770_2_1_1; -.
DR InParanoid; Q8RXE1; -.
DR OMA; MVATKFD; -.
DR OrthoDB; 481330at2759; -.
DR PhylomeDB; Q8RXE1; -.
DR UniPathway; UPA00845; -.
DR PRO; PR:Q8RXE1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8RXE1; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; IDA: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: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..610
FT /note="Probable galacturonosyltransferase 5"
FT /id="PRO_0000392558"
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..610
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 86..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 610 AA; 69886 MW; 7282D201E6F2EAC8 CRC64;
MNQVRRWQRI LILSLLLLSV LAPIVFVSNR LKSITSVDRG EFIEELSDIT DKTEDELRLT
AIEQDEEGLK EPKRILQDRD FNSVVLSNSS DKSNDTVQSN EGDQKNFLSE VDKGNNHKPK
EEQAVSQKTT VSSNAEVKIS ARDIQLNHKT EFRPPSSKSE KNTRVQLERA TDERVKEIRD
KIIQAKAYLN LALPGNNSQI VKELRVRTKE LERATGDTTK DKYLPKSSPN RLKAMEVALY
KVSRAFHNCP AIATKLQAMT YKTEEQARAQ KKQAAYLMQL AARTTPKGLH CLSMRLTTEY
FTLDHEKRQL LQQSYNDPDL YHYVVFSDNV LASSVVVNST ISSSKEPDKI VFHVVTDSLN
YPAISMWFLL NPSGRASIQI LNIDEMNVLP LYHAELLMKQ NSSDPRIISA LNHARFYLPD
IFPGLNKIVL FDHDVVVQRD LTRLWSLDMT GKVVGAVETC LEGDPSYRSM DSFINFSDAW
VSQKFDPKAC TWAFGMNLFD LEEWRRQELT SVYLKYFDLG VKGHLWKAGG LPVGWLTFFG
QTFPLEKRWN VGGLGHESGL RASDIEQAAV IHYDGIMKPW LDIGIDKYKR YWNIHVPYHH
PHLQRCNIHD
