B3GTG_ARATH
ID B3GTG_ARATH Reviewed; 619 AA.
AC Q9ASW1; Q4VWQ4; Q4VWQ5; Q9SQU7; W8QNR0;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Hydroxyproline O-galactosyltransferase GALT3 {ECO:0000303|PubMed:26690932};
DE EC=2.4.1.- {ECO:0000269|PubMed:26690932};
DE AltName: Full=Beta-1,3-galactosyltransferase 16 {ECO:0000305};
GN Name=GALT3 {ECO:0000303|PubMed:26690932};
GN Synonyms=B3GALT16 {ECO:0000305|PubMed:18548197};
GN OrderedLocusNames=At3g06440; ORFNames=F24P17.7;
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] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Wassilewskija;
RA Kiefer-Meyer M.-C., Faye L., Gomord V.;
RT "Arabidopsis thaliana putative beta 1,3 galactosyltransferase.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
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=2;
CC Name=1;
CC IsoId=Q9ASW1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ASW1-2; Sequence=VSP_036149, VSP_036150;
CC -!- TISSUE SPECIFICITY: Expressed in juvenile leaves, stems, cauline leaves
CC and siliques. {ECO:0000269|PubMed:17630273}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of arabinogalactan proteins. Root
CC hair defects. Reduced seed coat mucilage. Increased sensitivity to salt
CC stress. {ECO:0000269|PubMed:26690932}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF08572.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY305276; AAQ77230.1; -; mRNA.
DR EMBL; AY305277; AAQ77231.1; -; mRNA.
DR EMBL; KJ138838; AHL38778.1; -; mRNA.
DR EMBL; AC011623; AAF08572.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74393.1; -; Genomic_DNA.
DR EMBL; AF361640; AAK32808.1; -; mRNA.
DR EMBL; BT002218; AAN72229.1; -; mRNA.
DR RefSeq; NP_566284.1; NM_111519.3. [Q9ASW1-1]
DR AlphaFoldDB; Q9ASW1; -.
DR SMR; Q9ASW1; -.
DR STRING; 3702.AT3G06440.1; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; Q9ASW1; -.
DR EnsemblPlants; AT3G06440.1; AT3G06440.1; AT3G06440. [Q9ASW1-1]
DR GeneID; 819820; -.
DR Gramene; AT3G06440.1; AT3G06440.1; AT3G06440. [Q9ASW1-1]
DR KEGG; ath:AT3G06440; -.
DR Araport; AT3G06440; -.
DR TAIR; locus:2081071; AT3G06440.
DR eggNOG; KOG2287; Eukaryota.
DR HOGENOM; CLU_017063_1_0_1; -.
DR InParanoid; Q9ASW1; -.
DR OMA; LQKEHEP; -.
DR OrthoDB; 405234at2759; -.
DR PhylomeDB; Q9ASW1; -.
DR BioCyc; ARA:AT3G06440-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9ASW1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9ASW1; baseline and differential.
DR Genevisible; Q9ASW1; 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:0018258; P:protein O-linked glycosylation via hydroxyproline; IDA:UniProtKB.
DR GO; GO:0080147; P:root hair cell development; IMP:TAIR.
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..619
FT /note="Hydroxyproline O-galactosyltransferase GALT3"
FT /id="PRO_0000359426"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 21..37
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..619
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 166..344
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 552..559
FT /note="LFKLEDVA -> VSFVVSSP (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_036149"
FT VAR_SEQ 560..619
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_036150"
FT CONFLICT 2
FT /note="K -> Q (in Ref. 1; AAQ77230)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="N -> S (in Ref. 1; AAQ77231)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="R -> G (in Ref. 1; AAQ77230)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="R -> C (in Ref. 1; AAQ77230/AAQ77231)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="F -> S (in Ref. 1; AAQ77231)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="R -> W (in Ref. 1; AAQ77230)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="L -> I (in Ref. 1; AAQ77230)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="G -> E (in Ref. 1; AAQ77230)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="K -> T (in Ref. 1; AAQ77230/AAQ77231)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="V -> C (in Ref. 1; AAQ77231)"
FT /evidence="ECO:0000305"
FT CONFLICT 467..470
FT /note="KTDD -> MSGC (in Ref. 1; AAQ77231)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="N -> K (in Ref. 1; AAQ77231)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 70635 MW; 755F1DFC9ECFDBD8 CRC64;
MKQFMSVVRF KFGFTSVRMR DWSVGVSIMV LTLIFIIRYE QSDHTHTVDD SSIEGESVHE
PAKKPHFMTL EDLDYLFSNK SFFGEEEVSN GMLVWSRMRP FLERPDALPE TAQGIEEATL
AMKGLVLEIN REKRAYSSGM VSKEIRRICP DFVTAFDKDL SGLSHVLLEL PCGLIEDSSI
TLVGIPDEHS SSFQIQLVGS GLSGETRRPI ILRYNVNFSK PSIVQNTWTE KLGWGNEERC
QYHGSLKNHL VDELPLCNKQ TGRIISEKSS NDDATMELSL SNANFPFLKG SPFTAALWFG
LEGFHMTING RHETSFAYRE KLEPWLVSAV KVSGGLKILS VLATRLPIPD DHASLIIEEK
LKAPSLSGTR IELLVGVFST GNNFKRRMAL RRSWMQYEAV RSGKVAVRFL IGLHTNEKVN
LEMWRESKAY GDIQFMPFVD YYGLLSLKTV ALCILGTKVI PAKYIMKTDD DAFVRIDELL
SSLEERPSSA LLYGLISFDS SPDREQGSKW FIPKEEWPLD SYPPWAHGPG YIISHDIAKF
VVKGHRQRDL GLFKLEDVAM GIWIQQFNQT IKRVKYINDK RFHNSDCKSN YILVHYQTPR
LILCLWEKLQ KENQSICCE
