ID   GALS2_ARATH             Reviewed;         519 AA.
AC   Q9LTZ9;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Galactan beta-1,4-galactosyltransferase GALS2 {ECO:0000305};
DE            EC=2.4.1.- {ECO:0000305};
DE   AltName: Full=Beta-1,4-galactan synthase;
DE   AltName: Full=Galactan synthase 2 {ECO:0000303|PubMed:23243126};
GN   Name=GALS2 {ECO:0000303|PubMed:23243126};
GN   OrderedLocusNames=At5g44670 {ECO:0000312|Araport:AT5G44670};
GN   ORFNames=K15C23.12 {ECO:0000312|EMBL:BAA98120.1};
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;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
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 the midrib of mature leaves, root
CC       vasculature, flower filaments, siliques and seeds.
CC       {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}.
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DR   EMBL; KJ138650; AHL38590.1; -; mRNA.
DR   EMBL; AB024024; BAA98120.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95145.1; -; Genomic_DNA.
DR   EMBL; AF361577; AAK32745.1; -; mRNA.
DR   EMBL; BT002232; AAN72243.1; -; mRNA.
DR   RefSeq; NP_199280.1; NM_123834.2.
DR   AlphaFoldDB; Q9LTZ9; -.
DR   SMR; Q9LTZ9; -.
DR   STRING; 3702.AT5G44670.1; -.
DR   CAZy; GT92; Glycosyltransferase Family 92.
DR   PaxDb; Q9LTZ9; -.
DR   PRIDE; Q9LTZ9; -.
DR   ProteomicsDB; 228754; -.
DR   EnsemblPlants; AT5G44670.1; AT5G44670.1; AT5G44670.
DR   GeneID; 834496; -.
DR   Gramene; AT5G44670.1; AT5G44670.1; AT5G44670.
DR   KEGG; ath:AT5G44670; -.
DR   Araport; AT5G44670; -.
DR   TAIR; locus:2152130; AT5G44670.
DR   eggNOG; KOG4735; Eukaryota.
DR   HOGENOM; CLU_022400_2_0_1; -.
DR   InParanoid; Q9LTZ9; -.
DR   OMA; WAAYNFV; -.
DR   OrthoDB; 563565at2759; -.
DR   PhylomeDB; Q9LTZ9; -.
DR   PRO; PR:Q9LTZ9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LTZ9; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; HDA:TAIR.
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:0005773; C:vacuole; HDA:TAIR.
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..519
FT                   /note="Galactan beta-1,4-galactosyltransferase GALS2"
FT                   /id="PRO_0000435704"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          257..471
FT                   /note="GT92"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   519 AA;  59956 MW;  D93BDFA83946F6F7 CRC64;
     MAKERDQNTK DKNLLICFLW NFSAELKLAL MALLVLCTLA TLLPFLPSSF SISASELRFC
     ISRIAVNSTS VNFTTVVEKP VLDNAVKLTE KPVLDNGVTK QPLTEEKVLN NGVIKRTFTG
     YGWAAYNFVL MNAYRGGVNT FAVIGLSSKP LHVYSHPTYR CEWIPLNQSD NRILTDGTKI
     LTDWGYGRVY TTVVVNCTFP SNTVINPKNT GGTLLLHATT GDTDRNITDS IPVLTETPNT
     VDFALYESNL RRREKYDYLY CGSSLYGNLS PQRIREWIAY HVRFFGERSH FVLHDAGGIT
     EEVFEVLKPW IELGRVTVHD IREQERFDGY YHNQFMVVND CLHRYRFMAK WMFFFDVDEF
     IYVPAKSSIS SVMVSLEEYS QFTIEQMPMS SQLCYDGDGP ARTYRKWGFE KLAYRDVKKV
     PRRDRKYAVQ PRNVFATGVH MSQHLQGKTY HRAEGKIRYF HYHGSISQRR EPCRHLYNGT
     RIVHENNPYV LDTTMRDIGL AVKTFEIRTI GDRLLRTRQ