GOLS2_ARATH
ID GOLS2_ARATH Reviewed; 335 AA.
AC Q9FXB2; Q945L1;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Galactinol synthase 2;
DE Short=AtGolS2;
DE Short=GolS-2;
DE EC=2.4.1.123;
GN Name=GOLS2; OrderedLocusNames=At1g56600; ORFNames=F25P12.95;
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], FUNCTION, INDUCTION BY DROUGHT; ABA AND
RP HIGH-SALINITY STRESSES, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND GENE
RP FAMILY.
RX PubMed=11846875; DOI=10.1046/j.0960-7412.2001.01227.x;
RA Taji T., Ohsumi C., Iuchi S., Seki M., Kasuga M., Kobayashi M.,
RA Yamaguchi-Shinozaki K., Shinozaki K.;
RT "Important roles of drought- and cold-inducible genes for galactinol
RT synthase in stress tolerance in Arabidopsis thaliana.";
RL Plant J. 29:417-426(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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, INDUCTION BY METHYLVIOLOGEN, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18502973; DOI=10.1104/pp.108.122465;
RA Nishizawa A., Yabuta Y., Shigeoka S.;
RT "Galactinol and raffinose constitute a novel function to protect plants
RT from oxidative damage.";
RL Plant Physiol. 147:1251-1263(2008).
CC -!- FUNCTION: Galactinol synthase involved in the biosynthesis of raffinose
CC family oligosaccharides (RFOs) that function as osmoprotectants.
CC Promotes stress tolerance of factors such as drought, chilling,
CC salinity and methylviologen (MV), a superoxide radical generating drug,
CC by mediating an increase in levels of the endogenous osmoprotective
CC compounds, galactinol and raffinose. {ECO:0000269|PubMed:11846875,
CC ECO:0000269|PubMed:18502973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=myo-inositol + UDP-alpha-D-galactose = alpha-D-galactosyl-
CC (1->3)-1D-myo-inositol + H(+) + UDP; Xref=Rhea:RHEA:12464,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17268, ChEBI:CHEBI:17505,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.123;
CC Evidence={ECO:0000269|PubMed:11846875};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Accumulates in mature seeds.
CC {ECO:0000269|PubMed:11846875}.
CC -!- INDUCTION: Induced by abscisic acid (ABA), drought and high-salinity
CC stresses. Promoted by methylviologen (MV), a superoxide radical
CC generating drug, a superoxide radical generating drug.
CC {ECO:0000269|PubMed:11846875, ECO:0000269|PubMed:18502973}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC Galactosyltransferase subfamily. {ECO:0000305}.
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DR EMBL; AB062849; BAB78531.1; -; mRNA.
DR EMBL; AC009323; AAG09103.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33413.1; -; Genomic_DNA.
DR EMBL; AF412094; AAL06547.1; -; mRNA.
DR EMBL; AY050410; AAK91426.1; -; mRNA.
DR EMBL; AY058238; AAL15412.1; -; mRNA.
DR PIR; G96607; G96607.
DR RefSeq; NP_176053.1; NM_104537.3.
DR AlphaFoldDB; Q9FXB2; -.
DR SMR; Q9FXB2; -.
DR STRING; 3702.AT1G56600.1; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR PaxDb; Q9FXB2; -.
DR PRIDE; Q9FXB2; -.
DR ProteomicsDB; 247018; -.
DR EnsemblPlants; AT1G56600.1; AT1G56600.1; AT1G56600.
DR GeneID; 842114; -.
DR Gramene; AT1G56600.1; AT1G56600.1; AT1G56600.
DR KEGG; ath:AT1G56600; -.
DR Araport; AT1G56600; -.
DR TAIR; locus:2027549; AT1G56600.
DR eggNOG; KOG1950; Eukaryota.
DR HOGENOM; CLU_049943_3_0_1; -.
DR InParanoid; Q9FXB2; -.
DR OMA; TENITFM; -.
DR OrthoDB; 818680at2759; -.
DR PhylomeDB; Q9FXB2; -.
DR BioCyc; ARA:AT1G56600-MON; -.
DR BRENDA; 2.4.1.123; 399.
DR PRO; PR:Q9FXB2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FXB2; baseline and differential.
DR Genevisible; Q9FXB2; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0047216; F:inositol 3-alpha-galactosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006012; P:galactose metabolic process; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR030515; GOLS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11183:SF105; PTHR11183:SF105; 1.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Galactose metabolism;
KW Glycosyltransferase; Manganese; Metal-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..335
FT /note="Galactinol synthase 2"
FT /id="PRO_0000418658"
FT ACT_SITE 103
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
SQ SEQUENCE 335 AA; 38515 MW; 04F52C60B8A3F9D8 CRC64;
MAPEINTKLT VPVHSATGGE KRAYVTFLAG TGDYVKGVVG LAKGLRKAKS KYPLVVAVLP
DVPEDHRKQL VDQGCVVKEI EPVYPPENQT EFAMAYYVIN YSKLRIWEFV EYNKMIYLDG
DIQVFDNIDH LFDLPNGQFY AVMDCFCEKT WSHSPQYKIG YCQQCPDKVT WPEAKLGPKP
PLYFNAGMFV YEPNLSTYHN LLETVKIVPP TLFAEQDFLN MYFKDIYKPI PPVYNLVLAM
LWRHPENIEL DQVKVVHYCA AGAKPWRFTG EEENMDREDI KMLVKKWWDI YNDESLDYKN
VVIGDSHKKQ QTLQQFIEAL SEAGALQYVK APSAA
