B3GTK_ARATH
ID B3GTK_ARATH Reviewed; 684 AA.
AC A7XDQ9; Q9SUA8;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Hydroxyproline O-galactosyltransferase GALT2 {ECO:0000303|PubMed:23430255};
DE Short=AtGALT2 {ECO:0000303|PubMed:23430255};
DE EC=2.4.1.- {ECO:0000269|PubMed:23430255};
DE AltName: Full=Beta-1,3-galactosyltransferase 20 {ECO:0000305};
GN Name=GALT2 {ECO:0000303|PubMed:23430255};
GN Synonyms=B3GALT20 {ECO:0000305|PubMed:18548197};
GN OrderedLocusNames=At4g21060; ORFNames=T13K14.220;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 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, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=23430255; DOI=10.1074/jbc.m112.432609;
RA Basu D., Liang Y., Liu X., Himmeldirk K., Faik A., Kieliszewski M.,
RA Held M., Showalter A.M.;
RT "Functional identification of a hydroxyproline-o-galactosyltransferase
RT specific for arabinogalactan protein biosynthesis in Arabidopsis.";
RL J. Biol. Chem. 288:10132-10143(2013).
RN [6]
RP FUNCTION, COFACTOR, 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).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25974423; DOI=10.1371/journal.pone.0125624;
RA Basu D., Wang W., Ma S., DeBrosse T., Poirier E., Emch K., Soukup E.,
RA Tian L., Showalter A.M.;
RT "Two hydroxyproline galactosyltransferases, GALT5 and GALT2, function in
RT arabinogalactan-protein glycosylation, growth and development in
RT Arabidopsis.";
RL PLoS ONE 10:E0125624-E0125624(2015).
RN [8]
RP INDUCTION BY SALT STRESS.
RX PubMed=26731606; DOI=10.1371/journal.pone.0145092;
RA Basu D., Tian L., Debrosse T., Poirier E., Emch K., Herock H., Travers A.,
RA Showalter A.M.;
RT "Glycosylation of a fasciclin-like arabinogalactan-protein (SOS5) mediates
RT root growth and seed mucilage adherence via a cell wall receptor-like
RT kinase (FEI1/FEI2) pathway in Arabidopsis.";
RL PLoS ONE 11:E0145092-E0145092(2016).
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:23430255, ECO:0000269|PubMed:25974423,
CC ECO:0000269|PubMed:26690932}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:26690932};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:23430255};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:23430255}; 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=A7XDQ9-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in stems and at lower levels in cauline
CC leaves and siliques. {ECO:0000269|PubMed:17630273}.
CC -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:26731606}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of arabinogalactan proteins
CC (PubMed:26690932, PubMed:25974423). Defects in root hair growth, root
CC elongation, pollen tube growth, flowering time, leaf development,
CC silique length and inflorescence growth. Increased sensitivity to salt
CC stress (PubMed:25974423). {ECO:0000269|PubMed:25974423,
CC ECO:0000269|PubMed:26690932}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45901.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79106.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EF428438; ABR58857.1; -; mRNA.
DR EMBL; AL080282; CAB45901.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161554; CAB79106.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84393.1; -; Genomic_DNA.
DR PIR; T10648; T10648.
DR RefSeq; NP_001154260.1; NM_001160788.1. [A7XDQ9-1]
DR AlphaFoldDB; A7XDQ9; -.
DR SMR; A7XDQ9; -.
DR BioGRID; 13144; 4.
DR STRING; 3702.AT4G21060.1; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; A7XDQ9; -.
DR PRIDE; A7XDQ9; -.
DR ProteomicsDB; 241187; -. [A7XDQ9-1]
DR EnsemblPlants; AT4G21060.2; AT4G21060.2; AT4G21060. [A7XDQ9-1]
DR GeneID; 827853; -.
DR Gramene; AT4G21060.2; AT4G21060.2; AT4G21060. [A7XDQ9-1]
DR KEGG; ath:AT4G21060; -.
DR Araport; AT4G21060; -.
DR eggNOG; KOG2287; Eukaryota.
DR HOGENOM; CLU_017063_2_0_1; -.
DR InParanoid; A7XDQ9; -.
DR OMA; CMEDYFT; -.
DR PhylomeDB; A7XDQ9; -.
DR BioCyc; ARA:AT4G21060-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:A7XDQ9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; A7XDQ9; baseline and differential.
DR Genevisible; A7XDQ9; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
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:UniProtKB.
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 GO; GO:0080147; P:root hair cell development; IMP: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 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Manganese; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..684
FT /note="Hydroxyproline O-galactosyltransferase GALT2"
FT /id="PRO_0000359430"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 23..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..684
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 191..405
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT REGION 80..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 632
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 684 AA; 77912 MW; C877E82BDC30326A CRC64;
MKRVKSESFR GVYSSRRFKL SHFLLAIAGF YLVFLAFKFP HFIEMVAMLS GDTGLDGALS
DTSLDVSLSG SLRNDMLNRK LEDEDHQSGP STTQKVSPEE KINGSKQIQP LLFRYGRISG
EVMRRRNRTI HMSPFERMAD EAWILGSKAW EDVDKFEVDK INESASIFEG KVESCPSQIS
MNGDDLNKAN RIMLLPCGLA AGSSITILGT PQYAHKESVP QRSRLTRSYG MVLVSQFMVE
LQGLKTGDGE YPPKILHLNP RIKGDWNHRP VIEHNTCYRM QWGVAQRCDG TPSKKDADVL
VDGFRRCEKW TQNDIIDMVD SKESKTTSWF KRFIGREQKP EVTWSFPFAE GKVFVLTLRA
GIDGFHINVG GRHVSSFPYR PGFTIEDATG LAVTGDVDIH SIHATSLSTS HPSFSPQKAI
EFSSEWKAPP LPGTPFRLFM GVLSATNHFS ERMAVRKTWM QHPSIKSSDV VARFFVALNP
RKEVNAMLKK EAEYFGDIVI LPFMDRYELV VLKTIAICEF GVQNVTAPYI MKCDDDTFIR
VESILKQIDG VSPEKSLYMG NLNLRHRPLR TGKWTVTWEE WPEAVYPPYA NGPGYIISSN
IAKYIVSQNS RHKLRLFKME DVSMGLWVEQ FNASMQPVEY SHSWKFCQYG CTLNYYTAHY
QSPSQMMCLW DNLLKGRPQC CNFR
