B3GTH_ARATH
ID B3GTH_ARATH Reviewed; 673 AA.
AC Q8GXG6; Q9LFX6; W8Q7B2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Hydroxyproline O-galactosyltransferase GALT4 {ECO:0000303|PubMed:26690932};
DE EC=2.4.1.- {ECO:0000269|PubMed:26690932};
DE AltName: Full=Beta-1,3-galactosyltransferase 17 {ECO:0000305};
GN Name=GALT4 {ECO:0000303|PubMed:26690932};
GN Synonyms=B3GALT17 {ECO:0000305|PubMed:18548197};
GN OrderedLocusNames=At1g27120; ORFNames=T7N9.18;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=24905498; DOI=10.1111/tpj.12577;
RA Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for functional genomics.";
RL Plant J. 79:517-529(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=17630273; DOI=10.1105/tpc.107.052985;
RA Strasser R., Bondili J.S., Vavra U., Schoberer J., Svoboda B., Gloessl J.,
RA Leonard R., Stadlmann J., Altmann F., Steinkellner H., Mach L.;
RT "A unique beta-1,3-galactosyltransferase is indispensable for the
RT biosynthesis of N-glycans containing Lewis a structures in Arabidopsis
RT thaliana.";
RL Plant Cell 19:2278-2292(2007).
RN [6]
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 [7]
RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=26690932; DOI=10.1186/s12870-015-0670-7;
RA Basu D., Tian L., Wang W., Bobbs S., Herock H., Travers A., Showalter A.M.;
RT "A small multigene hydroxyproline-O-galactosyltransferase family functions
RT in arabinogalactan-protein glycosylation, growth and development in
RT Arabidopsis.";
RL BMC Plant Biol. 15:295-295(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. Utilizes UDP-galactose
CC solely as sugar donor. The addition of galactose onto the peptidyl
CC hydroxyproline residues in AGP core proteins represents the first
CC committed step in arabinogalactan polysaccharide addition. AGP glycans
CC play essential roles in both vegetative and reproductive plant growth.
CC {ECO:0000269|PubMed:26690932}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:26690932};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:26690932}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, cauline leaves and siliques.
CC {ECO:0000269|PubMed:17630273}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of arabinogalactan proteins. Root
CC hair defects. Reduced seed sets. Increased sensitivity to salt stress.
CC {ECO:0000269|PubMed:26690932}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79857.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KJ138984; AHL38924.1; -; mRNA.
DR EMBL; AC000348; AAF79857.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30783.1; -; Genomic_DNA.
DR EMBL; AK118254; BAC42872.1; -; mRNA.
DR PIR; G86397; G86397.
DR RefSeq; NP_174032.2; NM_102474.4.
DR AlphaFoldDB; Q8GXG6; -.
DR SMR; Q8GXG6; -.
DR BioGRID; 24836; 1.
DR IntAct; Q8GXG6; 1.
DR STRING; 3702.AT1G27120.1; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR iPTMnet; Q8GXG6; -.
DR PaxDb; Q8GXG6; -.
DR PRIDE; Q8GXG6; -.
DR ProteomicsDB; 240963; -.
DR EnsemblPlants; AT1G27120.1; AT1G27120.1; AT1G27120.
DR GeneID; 839601; -.
DR Gramene; AT1G27120.1; AT1G27120.1; AT1G27120.
DR KEGG; ath:AT1G27120; -.
DR Araport; AT1G27120; -.
DR TAIR; locus:2205774; AT1G27120.
DR eggNOG; KOG2287; Eukaryota.
DR HOGENOM; CLU_017063_2_0_1; -.
DR InParanoid; Q8GXG6; -.
DR OrthoDB; 292392at2759; -.
DR PhylomeDB; Q8GXG6; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q8GXG6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GXG6; baseline and differential.
DR Genevisible; Q8GXG6; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA: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:0030246; F:carbohydrate binding; IEA:InterPro.
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:0010405; P:arabinogalactan protein metabolic process; IMP:UniProtKB.
DR GO; GO:0018258; P:protein O-linked glycosylation via hydroxyproline; IDA:UniProtKB.
DR CDD; cd00070; GLECT; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001079; Galectin_CRD.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF00337; Gal-bind_lectin; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
DR SMART; SM00908; Gal-bind_lectin; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51304; GALECTIN; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..673
FT /note="Hydroxyproline O-galactosyltransferase GALT4"
FT /id="PRO_0000359427"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 20..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..673
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 185..394
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 460
FT /note="V -> A (in Ref. 4; BAC42872)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 673 AA; 77037 MW; 758489AD9DDC85E6 CRC64;
MKKSKLDNSS SQIRFGLVQF LLVVLLFYFL CMSFEIPFIF RTGSGSGSDD VSSSSFADAL
PRPMVVGGGS REANWVVGEE EEADPHRHFK DPGRVQLRLP ERKMREFKSV SEIFVNESFF
DNGGFSDEFS IFHKTAKHAI SMGRKMWDGL DSGLIKPDKA PVKTRIEKCP DMVSVSESEF
VNRSRILVLP CGLTLGSHIT VVATPHWAHV EKDGDKTAMV SQFMMELQGL KAVDGEDPPR
ILHFNPRIKG DWSGRPVIEQ NTCYRMQWGS GLRCDGRESS DDEEYVDGEV KCERWKRDDD
DGGNNGDDFD ESKKTWWLNR LMGRRKKMIT HDWDYPFAEG KLFVLTLRAG MEGYHISVNG
RHITSFPYRT GFVLEDATGL AVKGNIDVHS VYAASLPSTN PSFAPQKHLE MQRIWKAPSL
PQKPVELFIG ILSAGNHFAE RMAVRKSWMQ QKLVRSSKVV ARFFVALHAR KEVNVDLKKE
AEYFGDIVIV PYMDHYDLVV LKTVAICEYG VNTVAAKYVM KCDDDTFVRV DAVIQEAEKV
KGRESLYIGN INFNHKPLRT GKWAVTFEEW PEEYYPPYAN GPGYILSYDV AKFIVDDFEQ
KRLRLFKMED VSMGMWVEKF NETRPVAVVH SLKFCQFGCI EDYFTAHYQS PRQMICMWDK
LQRLGKPQCC NMR
