GALS1_ARATH
ID GALS1_ARATH Reviewed; 496 AA.
AC O22807;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Galactan beta-1,4-galactosyltransferase GALS1 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=Beta-1,4-galactan synthase;
DE AltName: Full=Galactan synthase 1 {ECO:0000303|PubMed:23243126};
GN Name=GALS1 {ECO:0000303|PubMed:23243126};
GN OrderedLocusNames=At2g33570 {ECO:0000312|Araport:AT2G33570};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP 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. Can
CC transfer galactose residues from UDP-galactose to beta-1,4-
CC galactopentaose in vitro. Forms specifically beta-1,4-galactosyl
CC linkages and can add successive beta-1,4-galactosyl residues to the
CC acceptor. Beta-1,4-galactans are abundant polysaccharides in plant cell
CC walls and are found as side-chain of rhamnogalacturonan I, which is a
CC major component of pectin. {ECO:0000269|PubMed:23243126}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:23243126}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in root vasculature, mature leaves,
CC trichomes, flowers, siliques 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 -!- MISCELLANEOUS: Plants over-expressing GALS1 have a strong increase in
CC beta-1,4-galactan content in leaf cell wall.
CC {ECO:0000269|PubMed:23243126}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 92 family.
CC {ECO:0000305}.
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DR EMBL; KJ138875; AHL38815.1; -; mRNA.
DR EMBL; AC002332; AAB80674.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08854.1; -; Genomic_DNA.
DR EMBL; AY140059; AAM98200.1; -; mRNA.
DR EMBL; BT008868; AAP68307.1; -; mRNA.
DR EMBL; AY084834; AAM61399.1; -; mRNA.
DR PIR; B84747; B84747.
DR RefSeq; NP_565768.1; NM_128917.5.
DR AlphaFoldDB; O22807; -.
DR STRING; 3702.AT2G33570.1; -.
DR CAZy; GT92; Glycosyltransferase Family 92.
DR PaxDb; O22807; -.
DR PRIDE; O22807; -.
DR ProteomicsDB; 230472; -.
DR EnsemblPlants; AT2G33570.1; AT2G33570.1; AT2G33570.
DR GeneID; 817922; -.
DR Gramene; AT2G33570.1; AT2G33570.1; AT2G33570.
DR KEGG; ath:AT2G33570; -.
DR Araport; AT2G33570; -.
DR TAIR; locus:2050982; AT2G33570.
DR eggNOG; KOG4735; Eukaryota.
DR HOGENOM; CLU_022400_0_0_1; -.
DR InParanoid; O22807; -.
DR OMA; RFSPPFQ; -.
DR OrthoDB; 618174at2759; -.
DR PhylomeDB; O22807; -.
DR PRO; PR:O22807; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22807; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; IDA: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:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IDA:TAIR.
DR GO; GO:0042546; P:cell wall biogenesis; IMP:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045489; P:pectin biosynthetic process; IDA:TAIR.
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..496
FT /note="Galactan beta-1,4-galactosyltransferase GALS1"
FT /id="PRO_0000435703"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 232..464
FT /note="GT92"
FT /evidence="ECO:0000255"
SQ SEQUENCE 496 AA; 56865 MW; 6DC17047DB6CACE3 CRC64;
MRKEVLPPVL STTTVCFEKK PIIATLLALS LVMIVWNLPP YYHNLISTAR PCSAVTTTTT
TTLLSSSNFT SAENFTTSLS TTTAAASQKY DSTPSDPNKR VFQPFGNAAA LFVLMGAYRG
GPTTFSVIGL ASKPIHVYGK PWYKCEWISN NGTSIRAKAQ KILPDWGYGR VYTVVVVNCT
FNSNPNSDNT GGKLILNAYY NESPKLFERF TTLEESAGIY DESKYSPPYQ YDYLYCGSSL
YGNVSASRMR EWMAYHAWFF GDKSHFVFHD AGGVSPEVRK VLEPWIRAGR VTVQNIRDQS
QYDGYYYNQF LIVNDCLHRY RYAANWTFFF DVDEYIYLPH GNTLESVLDE FSVNTQFTIE
QNPMSSVLCI NDSSQDYPRQ WGFEKLLFKD SRTKIRRDRK YAIQAKNAFA TGVHMSENIV
GKTLHKTETK IRYYHYHNTI TVHEELCREM LPNSAKKKVT LYNKLPYVYD DNMKKLVKTI
KEFEQKKLGT DVKNFS
