B3GTJ_ARATH
ID B3GTJ_ARATH Reviewed; 681 AA.
AC Q9LV16; W8Q690;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Hydroxyproline O-galactosyltransferase GALT6 {ECO:0000303|PubMed:26690932};
DE EC=2.4.1.- {ECO:0000269|PubMed:26690932};
DE AltName: Full=Beta-1,3-galactosyltransferase 19 {ECO:0000305};
GN Name=GALT6 {ECO:0000303|PubMed:26690932};
GN Synonyms=B3GALT19 {ECO:0000305|PubMed:18548197};
GN OrderedLocusNames=At5g62620; ORFNames=MRG21.3;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LV16-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in junveile leaves and stems, and at
CC lower levels in cauline leaves and siliques.
CC {ECO:0000269|PubMed:17630273}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of arabinogalactan proteins. Root
CC hair defects. Reduced seed sets. Reduced seed coat mucilage. Increased
CC sensitivity to salt stress. Premature senescence.
CC {ECO:0000269|PubMed:26690932}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97209.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BX831498; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; KJ138629; AHL38569.1; -; mRNA.
DR EMBL; AB020751; BAA97209.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97631.1; -; Genomic_DNA.
DR EMBL; BX831498; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_201068.1; NM_125657.5. [Q9LV16-1]
DR AlphaFoldDB; Q9LV16; -.
DR SMR; Q9LV16; -.
DR STRING; 3702.AT5G62620.1; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR iPTMnet; Q9LV16; -.
DR PaxDb; Q9LV16; -.
DR PRIDE; Q9LV16; -.
DR ProteomicsDB; 240964; -. [Q9LV16-1]
DR EnsemblPlants; AT5G62620.1; AT5G62620.1; AT5G62620. [Q9LV16-1]
DR GeneID; 836383; -.
DR Gramene; AT5G62620.1; AT5G62620.1; AT5G62620. [Q9LV16-1]
DR KEGG; ath:AT5G62620; -.
DR Araport; AT5G62620; -.
DR TAIR; locus:2172219; AT5G62620.
DR eggNOG; KOG2287; Eukaryota.
DR HOGENOM; CLU_017063_2_0_1; -.
DR InParanoid; Q9LV16; -.
DR PhylomeDB; Q9LV16; -.
DR BioCyc; ARA:AT5G62620-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9LV16; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LV16; baseline and differential.
DR Genevisible; Q9LV16; 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:0048354; P:mucilage biosynthetic process involved in seed coat development; IMP:TAIR.
DR GO; GO:1900056; P:negative regulation of leaf senescence; IMP:TAIR.
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 Alternative splicing; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Manganese; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..681
FT /note="Hydroxyproline O-galactosyltransferase GALT6"
FT /id="PRO_0000359429"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 29..49
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..681
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 187..401
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT REGION 57..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 681 AA; 77741 MW; 096DB0745ECDDE0B CRC64;
MRKPKLSKLE RLEKFDIFVS LSKQRSVQIL MAVGLLYMLL ITFEIPFVFK TGLSSLSQDP
LTRPEKHNSQ RELQERRAPT RPLKSLLYQE SQSESPAQGL RRRTRILSSL RFDPETFNPS
SKDGSVELHK SAKVAWEVGR KIWEELESGK TLKALEKEKK KKIEEHGTNS CSLSVSLTGS
DLLKRGNIME LPCGLTLGSH ITVVGKPRAA HSEKDPKISM LKEGDEAVKV SQFKLELQGL
KAVEGEEPPR ILHLNPRLKG DWSGKPVIEQ NTCYRMQWGS AQRCEGWRSR DDEETVDGQV
KCEKWARDDS ITSKEEESSK AASWWLSRLI GRSKKVTVEW PFPFTVDKLF VLTLSAGLEG
YHVSVDGKHV TSFPYRTGFT LEDATGLTIN GDIDVHSVFA GSLPTSHPSF SPQRHLELSS
NWQAPSLPDE QVDMFIGILS AGNHFAERMA VRRSWMQHKL VKSSKVVARF FVALHSRKEV
NVELKKEAEF FGDIVIVPYM DSYDLVVLKT VAICEYGAHQ LAAKFIMKCD DDTFVQVDAV
LSEAKKTPTD RSLYIGNINY YHKPLRQGKW SVTYEEWPEE DYPPYANGPG YILSNDISRF
IVKEFEKHKL RMFKMEDVSV GMWVEQFNNG TKPVDYIHSL RFCQFGCIEN YLTAHYQSPR
QMICLWDKLV LTGKPQCCNM R
