B3GTB_ARATH
ID B3GTB_ARATH Reviewed; 338 AA.
AC Q94F27; Q2V2Z0; Q9FK08;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Hydroxyproline O-galactosyltransferase HPGT1 {ECO:0000303|PubMed:25600942};
DE EC=2.4.1.- {ECO:0000269|PubMed:25600942};
DE AltName: Full=Beta-1,3-galactosyltransferase 11 {ECO:0000305};
GN Name=HPTG1 {ECO:0000303|PubMed:25600942};
GN Synonyms=B3GALT11 {ECO:0000305|PubMed:18548197};
GN OrderedLocusNames=At5g53340; ORFNames=K19E1.14;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(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] (ISOFORM 1).
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=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 IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP 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:0000269|PubMed:25600942}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94F27-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94F27-2; Sequence=VSP_036148;
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 -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09796.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB013388; BAB09796.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96341.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96342.1; -; Genomic_DNA.
DR EMBL; AF386942; AAK62387.1; -; mRNA.
DR EMBL; AY081533; AAM10095.1; -; mRNA.
DR RefSeq; NP_001032067.1; NM_001036990.2. [Q94F27-2]
DR RefSeq; NP_568791.1; NM_124713.4. [Q94F27-1]
DR AlphaFoldDB; Q94F27; -.
DR SMR; Q94F27; -.
DR STRING; 3702.AT5G53340.1; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; Q94F27; -.
DR PRIDE; Q94F27; -.
DR ProteomicsDB; 241182; -. [Q94F27-1]
DR EnsemblPlants; AT5G53340.1; AT5G53340.1; AT5G53340. [Q94F27-1]
DR EnsemblPlants; AT5G53340.2; AT5G53340.2; AT5G53340. [Q94F27-2]
DR GeneID; 835415; -.
DR Gramene; AT5G53340.1; AT5G53340.1; AT5G53340. [Q94F27-1]
DR Gramene; AT5G53340.2; AT5G53340.2; AT5G53340. [Q94F27-2]
DR KEGG; ath:AT5G53340; -.
DR Araport; AT5G53340; -.
DR TAIR; locus:2154247; AT5G53340.
DR eggNOG; KOG2288; Eukaryota.
DR InParanoid; Q94F27; -.
DR OMA; TYETNGT; -.
DR PhylomeDB; Q94F27; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q94F27; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94F27; baseline and differential.
DR Genevisible; Q94F27; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005797; C:Golgi medial cisterna; HDA:TAIR.
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:0005802; C:trans-Golgi network; HDA:TAIR.
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 1: Evidence at protein level;
KW Alternative splicing; Glycosyltransferase; Golgi apparatus; Manganese;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..338
FT /note="Hydroxyproline O-galactosyltransferase HPGT1"
FT /id="PRO_0000359421"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 13..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..338
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT VAR_SEQ 332
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036148"
SQ SEQUENCE 338 AA; 37768 MW; 613C2D79C82A2E39 CRC64;
MARKGSSIRL SSSRISTLLL FMFATFASFY VAGRLWQESQ TRVHLINELD RVTGQGKSAI
SVDDTLKIIA CREQKKTLAA LEMELSSARQ EGFVSKSPKL ADGTETKKRP LVVIGIMTSL
GNKKKRDAVR QAWMGTGASL KKLESEKGVI ARFVIGRSAN KGDSMDKSID TENSQTDDFI
ILDDVVEAPE EASKKVKLFF AYAADRWDAQ FYAKAIDNIY VNIDALGTTL AAHLENPRAY
IGCMKSGEVF SEPNHKWYEP EWWKFGDKKA YFRHAYGEMY VITHALARFV SINRDILHSY
AHDDVSTGSW FVGLDVKHVD EGKFCCSAWS SEAICAGV