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GOLS3_ARATH
ID   GOLS3_ARATH             Reviewed;         334 AA.
AC   O80518;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Galactinol synthase 3;
DE            Short=AtGolS3;
DE            Short=GolS-3;
DE            EC=2.4.1.123;
GN   Name=GOLS3; OrderedLocusNames=At1g09350; ORFNames=F14J9.1;
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], INDUCTION BY COLD, CATALYTIC ACTIVITY, 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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
RN   [6]
RP   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).
RN   [7]
RP   INDUCTION BY COLD.
RX   PubMed=19500304; DOI=10.1111/j.1365-313x.2009.03938.x;
RA   Kwon C.S., Lee D., Choi G., Chung W.I.;
RT   "Histone occupancy-dependent and -independent removal of H3K27
RT   trimethylation at cold-responsive genes in Arabidopsis.";
RL   Plant J. 60:112-121(2009).
CC   -!- FUNCTION: Galactinol synthase involved in the biosynthesis of raffinose
CC       family oligosaccharides (RFOs) that function as osmoprotectants. May
CC       promote plant stress tolerance (By similarity). {ECO:0000250}.
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   -!- INDUCTION: Induced by cold in a DREB1A-dependent manner; this induction
CC       is accompanied by a reduction in trimethylation of 'Lys-27' of histone
CC       H3 (H3K27me3) in GOLS3 promoter (PubMed:19500304). Induced by
CC       methylviologen (MV), a superoxide radical generating drug.
CC       {ECO:0000269|PubMed:11846875, ECO:0000269|PubMed:18502973,
CC       ECO:0000269|PubMed:19500304}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC       Galactosyltransferase subfamily. {ECO:0000305}.
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DR   EMBL; AB062850; BAB78532.1; -; mRNA.
DR   EMBL; AC003970; AAC33195.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28432.1; -; Genomic_DNA.
DR   EMBL; AF370546; AAK48973.1; -; mRNA.
DR   EMBL; AY081452; AAM10014.1; -; mRNA.
DR   PIR; F86226; F86226.
DR   RefSeq; NP_172406.1; NM_100805.2.
DR   AlphaFoldDB; O80518; -.
DR   SMR; O80518; -.
DR   STRING; 3702.AT1G09350.1; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   PaxDb; O80518; -.
DR   PRIDE; O80518; -.
DR   EnsemblPlants; AT1G09350.1; AT1G09350.1; AT1G09350.
DR   GeneID; 837457; -.
DR   Gramene; AT1G09350.1; AT1G09350.1; AT1G09350.
DR   KEGG; ath:AT1G09350; -.
DR   Araport; AT1G09350; -.
DR   TAIR; locus:2012320; AT1G09350.
DR   eggNOG; KOG1950; Eukaryota.
DR   HOGENOM; CLU_049943_3_0_1; -.
DR   InParanoid; O80518; -.
DR   OMA; VSPDPCQ; -.
DR   OrthoDB; 818680at2759; -.
DR   PhylomeDB; O80518; -.
DR   BRENDA; 2.4.1.123; 399.
DR   PRO; PR:O80518; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O80518; baseline and differential.
DR   Genevisible; O80518; 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; ISS:UniProtKB.
DR   GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
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..334
FT                   /note="Galactinol synthase 3"
FT                   /id="PRO_0000418659"
FT   ACT_SITE        97
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         251
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   334 AA;  38677 MW;  0D09CA497B392BA2 CRC64;
     MAPEMNNKLS YGEKKRAYVT FLAGTGDYVK GVVGLAKGLR KTKSKYPLVV AVLPDVPADH
     RRQLLDQGCV IKEIQPVYPP DNQTQFAMAY YVLNYSKLRI WKFVEYSKLI YLDGDIQVFE
     NIDHLFDLPD GNFYAVKDCF CEKTWSHTPQ YKIGYCQQCP DKVTWPESEL GPKPPLYFNA
     GMFVYEPSLP TYYNLLETLK VVPPTPFAEQ DFLNMYFKDI YKPIPPVYNL VLAMLWRHPE
     NIELNEAKVV HYCAAGAKPW RFTGQEGNME REDIKMLVEK WWDIYNDESL DYKNFNVHCG
     QKEDVHRKPK TLPQFFTDLS EADVLQCAKA PSAA
 
 
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