GAUT4_ARATH
ID GAUT4_ARATH Reviewed; 616 AA.
AC Q93ZX7; Q9FIK3;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable galacturonosyltransferase 4;
DE EC=2.4.1.-;
DE AltName: Full=Like glycosyl transferase 3;
GN Name=GAUT4; Synonyms=JS36L, LGT3; OrderedLocusNames=At5g47780;
GN ORFNames=MCA23.10;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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.
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 -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11325.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB016886; BAB11325.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED95571.1; -; Genomic_DNA.
DR EMBL; AY056202; AAL07051.1; -; mRNA.
DR EMBL; AY091394; AAM14333.1; -; mRNA.
DR RefSeq; NP_568688.1; NM_124152.3.
DR AlphaFoldDB; Q93ZX7; -.
DR SMR; Q93ZX7; -.
DR BioGRID; 20077; 1.
DR STRING; 3702.AT5G47780.1; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR PaxDb; Q93ZX7; -.
DR PRIDE; Q93ZX7; -.
DR ProteomicsDB; 221903; -.
DR EnsemblPlants; AT5G47780.1; AT5G47780.1; AT5G47780.
DR GeneID; 834829; -.
DR Gramene; AT5G47780.1; AT5G47780.1; AT5G47780.
DR KEGG; ath:AT5G47780; -.
DR Araport; AT5G47780; -.
DR TAIR; locus:2160957; AT5G47780.
DR eggNOG; ENOG502QQZJ; Eukaryota.
DR HOGENOM; CLU_010770_2_1_1; -.
DR InParanoid; Q93ZX7; -.
DR OMA; HERQLWK; -.
DR OrthoDB; 290395at2759; -.
DR PhylomeDB; Q93ZX7; -.
DR UniPathway; UPA00845; -.
DR PRO; PR:Q93ZX7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93ZX7; baseline and differential.
DR Genevisible; Q93ZX7; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000137; C:Golgi cis 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: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; 2.
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..616
FT /note="Probable galacturonosyltransferase 4"
FT /id="PRO_0000392557"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..616
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 132..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 616 AA; 71149 MW; 0D28865F64B86577 CRC64;
MMVKLRNLVL FFMLLTVVAH ILLYTDPAAS FKTPFSKRDF LEDVTALTFN SDENRLNLLP
RESPAVLRGG LVGAVYSDKN SRRLDQLSAR VLSATDDDTH SHTDISIKQV THDAASDSHI
NRENMHVQLT QQTSEKVDEQ PEPNAFGAKK DTGNVLMPDA QVRHLKDQLI RAKVYLSLPS
AKANAHFVRE LRLRIKEVQR ALADASKDSD LPKTAIEKLK AMEQTLAKGK QIQDDCSTVV
KKLRAMLHSA DEQLRVHKKQ TMFLTQLTAK TIPKGLHCLP LRLTTDYYAL NSSEQQFPNQ
EKLEDTQLYH YALFSDNVLA TSVVVNSTIT NAKHPLKHVF HIVTDRLNYA AMRMWFLDNP
PGKATIQVQN VEEFTWLNSS YSPVLKQLSS RSMIDYYFRA HHTNSDTNLK FRNPKYLSIL
NHLRFYLPEI FPKLSKVLFL DDDIVVQKDL SGLWSVDLKG NVNGAVETCG ESFHRFDRYL
NFSNPLISKN FDPRACGWAY GMNVFDLDEW KRQNITEVYH RWQDLNQDRE LWKLGTLPPG
LITFWRRTYP LDRKWHILGL GYNPSVNQRD IERAAVIHYN GNLKPWLEIG IPRYRGFWSK
HVDYEHVYLR ECNINP
