ID   GALS3_ARATH             Reviewed;         504 AA.
AC   O65431; Q93Z06;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Galactan beta-1,4-galactosyltransferase GALS3 {ECO:0000305};
DE            EC=2.4.1.- {ECO:0000305};
DE   AltName: Full=Beta-1,4-galactan synthase;
DE   AltName: Full=Galactan synthase 3 {ECO:0000303|PubMed:23243126};
GN   Name=GALS3 {ECO:0000303|PubMed:23243126};
GN   OrderedLocusNames=At4g20170 {ECO:0000312|Araport:AT4G20170};
GN   ORFNames=F1C12.90 {ECO:0000312|EMBL:CAA18242.1};
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=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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=23243126; DOI=10.1105/tpc.112.106625;
RA   Liwanag A.J., Ebert B., Verhertbruggen Y., Rennie E.A., Rautengarten C.,
RA   Oikawa A., Andersen M.C., Clausen M.H., Scheller H.V.;
RT   "Pectin biosynthesis: GALS1 in Arabidopsis thaliana is a beta-1,4-galactan
RT   beta-1,4-galactosyltransferase.";
RL   Plant Cell 24:5024-5036(2012).
CC   -!- FUNCTION: Involved in the biosynthesis of beta-1,4-galactan. Beta-1,4-
CC       galactans are abundant polysaccharides in plant cell walls and are
CC       found as side-chain of rhamnogalacturonan I, which is a major component
CC       of pectin. {ECO:0000269|PubMed:23243126}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:O22807}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in root caps, mature leaves, top of the
CC       stems and seeds. {ECO:0000269|PubMed:23243126}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant plants have reduced content of beta-1,4-galactan
CC       in leaf cell wall. {ECO:0000269|PubMed:23243126}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 92 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL24253.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; KJ138743; AHL38683.1; -; mRNA.
DR   EMBL; AL022224; CAA18242.1; -; Genomic_DNA.
DR   EMBL; AL161552; CAB79017.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84282.1; -; Genomic_DNA.
DR   EMBL; AY058866; AAL24253.1; ALT_FRAME; mRNA.
DR   EMBL; BT000570; AAN18139.1; -; mRNA.
DR   PIR; T05325; T05325.
DR   RefSeq; NP_193750.1; NM_118136.4.
DR   AlphaFoldDB; O65431; -.
DR   STRING; 3702.AT4G20170.1; -.
DR   CAZy; GT92; Glycosyltransferase Family 92.
DR   PaxDb; O65431; -.
DR   PRIDE; O65431; -.
DR   ProteomicsDB; 248476; -.
DR   EnsemblPlants; AT4G20170.1; AT4G20170.1; AT4G20170.
DR   GeneID; 827763; -.
DR   Gramene; AT4G20170.1; AT4G20170.1; AT4G20170.
DR   KEGG; ath:AT4G20170; -.
DR   Araport; AT4G20170; -.
DR   TAIR; locus:2120387; AT4G20170.
DR   eggNOG; KOG4735; Eukaryota.
DR   HOGENOM; CLU_022400_2_0_1; -.
DR   InParanoid; O65431; -.
DR   OMA; YNFISMS; -.
DR   OrthoDB; 563565at2759; -.
DR   PhylomeDB; O65431; -.
DR   PRO; PR:O65431; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O65431; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042546; P:cell wall biogenesis; IMP:TAIR.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR008166; Glyco_transf_92.
DR   Pfam; PF01697; Glyco_transf_92; 1.
PE   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..504
FT                   /note="Galactan beta-1,4-galactosyltransferase GALS3"
FT                   /id="PRO_0000435705"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          242..456
FT                   /note="GT92"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   504 AA;  57783 MW;  D620DC57A7F33441 CRC64;
     MAMVKEKEQN TKDKKLLVGV IWNFSAELKL TFMALLVLCT LATLLPFIPS SFSLSTSDFR
     FCISRFSSAV PLNTTTTVEE SSSSPSPEKN LDRVLDNGVI KRTFTGYGSA AYNFVSMSAY
     RGGVNSFAVI GLSSKPLHVY GHPSYRCEWV SLDPTQDPIS TTGFKILTDW GYGRIYTTVV
     VNCTFSSISA VNPQNSGGTL ILHATTGDPT LNLTDSISVL TEPPKSVDFD LYNSTKKTKK
     YDYLYCGSSL YGNLSPQRVR EWIAYHVRFF GERSHFVLHD AGGIHEEVFE VLKPWIELGR
     VTLHDIRDQE RFDGYYHNQF MIVNDCLHRY RFMTKWMFFF DVDEFLHVPV KETISSVMES
     LEEYSQFTIE QMPMSSRICY SGDGPARTYR KWGIEKLAYR DVKKVPRRDR KYAVQPENVF
     ATGVHMSQNL QGKTYHKAES KIRYFHYHGS ISQRREPCRQ LFNDSRVVFE NTPYVLDTTI
     CDVGLAVRTF ELRTIGDRLL RTRQ