B3GT9_ARATH
ID B3GT9_ARATH Reviewed; 346 AA.
AC Q5XEZ1; Q9SIR3;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Hydroxyproline O-galactosyltransferase HPGT3 {ECO:0000303|PubMed:25600942};
DE EC=2.4.1.- {ECO:0000269|PubMed:25600942};
DE AltName: Full=Beta-1,3-galactosyltransferase 9 {ECO:0000305};
GN Name=HPGT3 {ECO:0000303|PubMed:25600942};
GN Synonyms=B3GALT9 {ECO:0000305|PubMed:18548197};
GN OrderedLocusNames=At2g25300; ORFNames=T22F11.11;
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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18548197; DOI=10.1007/s11103-008-9351-3;
RA Qu Y., Egelund J., Gilson P.R., Houghton F., Gleeson P.A., Schultz C.J.,
RA Bacic A.;
RT "Identification of a novel group of putative Arabidopsis thaliana beta-
RT (1,3)-galactosyltransferases.";
RL Plant Mol. Biol. 68:43-59(2008).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25600942; DOI=10.1111/tpj.12764;
RA Ogawa-Ohnishi M., Matsubayashi Y.;
RT "Identification of three potent hydroxyproline O-galactosyltransferases in
RT Arabidopsis.";
RL Plant J. 81:736-746(2015).
CC -!- FUNCTION: Possesses hydroxyproline O-galactosyltransferase activity.
CC Transfers galactose from UDP-galactose to hydroxyproline residues in
CC the arabinogalactan proteins (AGPs). Is specific for AGPs containing
CC non-contiguous peptidyl hydroxyproline residues. The addition of
CC galactose onto the peptidyl hydroxyproline residues in AGP core
CC proteins represents the first committed step in arabinogalactan
CC polysaccharide addition. AGP glycans play essential roles in both
CC vegetative and reproductive plant growth.
CC {ECO:0000269|PubMed:25600942}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A7XDQ9};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q94F27}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, cauline leaves,
CC stems, flowers and siliques. {ECO:0000269|PubMed:25600942}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of arabinogalactan proteins.
CC {ECO:0000269|PubMed:25600942}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD23661.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007070; AAD23661.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07684.1; -; Genomic_DNA.
DR EMBL; BT015825; AAU94388.1; -; mRNA.
DR EMBL; BT020527; AAW50705.1; -; mRNA.
DR PIR; G84646; G84646.
DR RefSeq; NP_180102.3; NM_128087.4.
DR AlphaFoldDB; Q5XEZ1; -.
DR SMR; Q5XEZ1; -.
DR BioGRID; 2420; 1.
DR STRING; 3702.AT2G25300.1; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; Q5XEZ1; -.
DR PRIDE; Q5XEZ1; -.
DR ProteomicsDB; 241181; -.
DR EnsemblPlants; AT2G25300.1; AT2G25300.1; AT2G25300.
DR GeneID; 817068; -.
DR Gramene; AT2G25300.1; AT2G25300.1; AT2G25300.
DR KEGG; ath:AT2G25300; -.
DR Araport; AT2G25300; -.
DR TAIR; locus:2059531; AT2G25300.
DR eggNOG; KOG2288; Eukaryota.
DR HOGENOM; CLU_040730_1_0_1; -.
DR InParanoid; Q5XEZ1; -.
DR OrthoDB; 640360at2759; -.
DR PhylomeDB; Q5XEZ1; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q5XEZ1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q5XEZ1; baseline and differential.
DR Genevisible; Q5XEZ1; AT.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008378; F:galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:1990714; F:hydroxyproline O-galactosyltransferase activity; IDA:TAIR.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0010405; P:arabinogalactan protein metabolic process; IMP:UniProtKB.
DR GO; GO:0018258; P:protein O-linked glycosylation via hydroxyproline; IDA:UniProtKB.
DR InterPro; IPR025298; DUF4094.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF13334; DUF4094; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 2: Evidence at transcript level;
KW Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..346
FT /note="Hydroxyproline O-galactosyltransferase HPGT3"
FT /id="PRO_0000359419"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 29..45
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..346
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 346 AA; 39059 MW; CBDAA9846A4032DA CRC64;
MESLPTTVPS KSERRARSSK FSQSSSKPSV IMAFFSCVAW LYVAGRLWQD AENRVVLNNI
LKKSYDQKPK VLTVDDKLMV LGCKDLERRI VETEMELTLA KSQGYLKNLK SGSSSGKKLL
AVIGVYSGFG SHLRRNTFRG SYMPQGDALR KLEERGIVIR FVIGRSPNRG DSLDRKIDEE
NQARKDFLIL ENHEEAQEEL AKKVKFFFSA AVQNWDAEFY IKVDDNIDLD LEGLIGLLES
RRGQDAAYIG CMKSGEVVAE EGGKWYEPEW WKFGDEKSYF RHAAGSLLIL SKTLAQYVNI
NSGSLKTYAF DDTSIGSWMI GVQATYIDDN RLCCSSIRQD KVCSVA
