TPS1_ARATH
ID TPS1_ARATH Reviewed; 942 AA.
AC Q9SYM4; P93653; Q94K55;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 1 {ECO:0000305};
DE EC=2.4.1.15 {ECO:0000269|PubMed:11520870};
DE AltName: Full=Trehalose-6-phosphate synthase 1 {ECO:0000303|PubMed:9681010};
DE Short=AtTPS1 {ECO:0000303|PubMed:9681010};
GN Name=TPS1 {ECO:0000303|PubMed:9681010};
GN OrderedLocusNames=At1g78580 {ECO:0000312|Araport:AT1G78580};
GN ORFNames=T30F21.9 {ECO:0000312|EMBL:AAD30578.1};
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], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9681010; DOI=10.1046/j.1365-313x.1998.00063.x;
RA Blazquez M.A., Santos E., Flores C.L., Martinez-Zapater J.M., Salinas J.,
RA Gancedo C.;
RT "Isolation and molecular characterization of the Arabidopsis TPS1 gene,
RT encoding trehalose-6-phosphate synthase.";
RL Plant J. 13:685-689(1998).
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] OF 389-942.
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11701378; DOI=10.1016/s1360-1385(01)02125-2;
RA Leyman B., Van Dijck P., Thevelein J.M.;
RT "An unexpected plethora of trehalose biosynthesis genes in Arabidopsis
RT thaliana.";
RL Trends Plant Sci. 6:510-513(2001).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11520870; DOI=10.1093/jexbot/52.362.1817;
RA Vogel G., Fiehn O., Jean-Richard-dit-Bressel L., Boller T., Wiemken A.,
RA Aeschbacher R.A., Wingler A.;
RT "Trehalose metabolism in Arabidopsis: occurrence of trehalose and molecular
RT cloning and characterization of trehalose-6-phosphate synthase
RT homologues.";
RL J. Exp. Bot. 52:1817-1826(2001).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF ARG-17 AND LEU-27.
RX PubMed=11978181; DOI=10.1042/bj20020517;
RA Van Dijck P., Mascorro-Gallardo J.O., De Bus M., Royackers K.,
RA Iturriaga G., Thevelein J.M.;
RT "Truncation of Arabidopsis thaliana and Selaginella lepidophylla trehalose-
RT 6-phosphate synthase unlocks high catalytic activity and supports high
RT trehalose levels on expression in yeast.";
RL Biochem. J. 366:63-71(2002).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=11851922; DOI=10.1046/j.1365-313x.2002.01220.x;
RA Eastmond P.J., van Dijken A.J.H., Spielman M., Kerr A., Tissier A.F.,
RA Dickinson H.G., Jones J.D.G., Smeekens S.C., Graham I.A.;
RT "Trehalose-6-phosphate synthase 1, which catalyses the first step in
RT trehalose synthesis, is essential for Arabidopsis embryo maturation.";
RL Plant J. 29:225-235(2002).
RN [9]
RP FUNCTION.
RX PubMed=12748379; DOI=10.1073/pnas.1132018100;
RA Schluepmann H., Pellny T., van Dijken A.J.H., Smeekens S.C.M., Paul M.;
RT "Trehalose 6-phosphate is indispensable for carbohydrate utilization and
RT growth in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:6849-6854(2003).
RN [10]
RP INDUCTION BY SUCROSE.
RX PubMed=15181209; DOI=10.1104/pp.104.039503;
RA Schluepmann H., van Dijken A.J.H., Aghdasi M., Wobbes B., Paul M.,
RA Smeekens S.C.M.;
RT "Trehalose mediated growth inhibition of Arabidopsis seedlings is due to
RT trehalose-6-phosphate accumulation.";
RL Plant Physiol. 135:879-890(2004).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15181208; DOI=10.1104/pp.104.039743;
RA van Dijken A.J.H., Schluepmann H., Smeekens S.C.M.;
RT "Arabidopsis trehalose-6-phosphate synthase 1 is essential for normal
RT vegetative growth and transition to flowering.";
RL Plant Physiol. 135:969-977(2004).
RN [12]
RP FUNCTION.
RX PubMed=15667325; DOI=10.1042/bst0330276;
RA Avonce N., Leyman B., Thevelein J., Iturriaga G.;
RT "Trehalose metabolism and glucose sensing in plants.";
RL Biochem. Soc. Trans. 33:276-279(2005).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15667326; DOI=10.1042/bst0330280;
RA Gomez L.D., Baud S., Graham I.A.;
RT "The role of trehalose-6-phosphate synthase in Arabidopsis embryo
RT development.";
RL Biochem. Soc. Trans. 33:280-282(2005).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16553896; DOI=10.1111/j.1365-313x.2006.02662.x;
RA Gomez L.D., Baud S., Gilday A., Li Y., Graham I.A.;
RT "Delayed embryo development in the ARABIDOPSIS TREHALOSE-6-PHOSPHATE
RT SYNTHASE 1 mutant is associated with altered cell wall structure, decreased
RT cell division and starch accumulation.";
RL Plant J. 46:69-84(2006).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=17111094; DOI=10.1007/s00709-006-0198-7;
RA Almeida A.M., Santos M., Villalobos E., Araujo S.S., van Dijck P.,
RA Leyman B., Cardoso L.A., Santos D., Fevereiro P.S., Torne J.M.;
RT "Immunogold localization of trehalose-6-phosphate synthase in leaf segments
RT of wild-type and transgenic tobacco plants expressing the AtTPS1 gene from
RT Arabidopsis thaliana.";
RL Protoplasma 230:41-49(2007).
CC -!- FUNCTION: Required for normal embryo development, vegetative growth and
CC transition to flowering. Regulates embryo growth, cell wall deposition,
CC starch and sucrose degradation, but not cell differentiation. Involved
CC in the regulation of glucose sensing and signaling genes during plant
CC development. {ECO:0000269|PubMed:11520870, ECO:0000269|PubMed:11851922,
CC ECO:0000269|PubMed:11978181, ECO:0000269|PubMed:12748379,
CC ECO:0000269|PubMed:15181208, ECO:0000269|PubMed:15667325,
CC ECO:0000269|PubMed:15667326, ECO:0000269|PubMed:16553896,
CC ECO:0000269|PubMed:9681010}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-
CC trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15;
CC Evidence={ECO:0000269|PubMed:11520870};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18890;
CC Evidence={ECO:0000269|PubMed:11520870};
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:17111094}. Secreted,
CC cell wall {ECO:0000269|PubMed:17111094}. Cytoplasm
CC {ECO:0000269|PubMed:17111094}. Note=Determined in transgenic tobacco
CC plants expressing TPS1.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, roots, stems,
CC flowers and siliques. {ECO:0000269|PubMed:11520870,
CC ECO:0000269|PubMed:11851922, ECO:0000269|PubMed:9681010}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during seed development.
CC {ECO:0000269|PubMed:11851922}.
CC -!- INDUCTION: Low induction by sucrose after 24 hours. Down-regulated by
CC dark incubation. {ECO:0000269|PubMed:11520870,
CC ECO:0000269|PubMed:15181209}.
CC -!- DOMAIN: The N-terminal part (1-88) has an inhibitory function on the
CC enzymatic activity.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality.
CC {ECO:0000269|PubMed:11851922, ECO:0000269|PubMed:15181208,
CC ECO:0000269|PubMed:15667326, ECO:0000269|PubMed:16553896}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 20 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the trehalose
CC phosphatase family. {ECO:0000305}.
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DR EMBL; Y08568; CAA69879.1; -; mRNA.
DR EMBL; AC007260; AAD30578.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36123.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60660.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60661.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60662.1; -; Genomic_DNA.
DR EMBL; AF370287; AAK44102.2; -; mRNA.
DR PIR; D96814; D96814.
DR RefSeq; NP_001319403.1; NM_001334832.1.
DR RefSeq; NP_001322931.1; NM_001334833.1.
DR RefSeq; NP_001322932.1; NM_001334834.1.
DR RefSeq; NP_177979.1; NM_106505.5.
DR AlphaFoldDB; Q9SYM4; -.
DR SMR; Q9SYM4; -.
DR STRING; 3702.AT1G78580.1; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR iPTMnet; Q9SYM4; -.
DR PaxDb; Q9SYM4; -.
DR PRIDE; Q9SYM4; -.
DR ProteomicsDB; 232494; -.
DR EnsemblPlants; AT1G78580.1; AT1G78580.1; AT1G78580.
DR EnsemblPlants; AT1G78580.2; AT1G78580.2; AT1G78580.
DR EnsemblPlants; AT1G78580.3; AT1G78580.3; AT1G78580.
DR EnsemblPlants; AT1G78580.4; AT1G78580.4; AT1G78580.
DR GeneID; 844194; -.
DR Gramene; AT1G78580.1; AT1G78580.1; AT1G78580.
DR Gramene; AT1G78580.2; AT1G78580.2; AT1G78580.
DR Gramene; AT1G78580.3; AT1G78580.3; AT1G78580.
DR Gramene; AT1G78580.4; AT1G78580.4; AT1G78580.
DR KEGG; ath:AT1G78580; -.
DR Araport; AT1G78580; -.
DR TAIR; locus:2202990; AT1G78580.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_0_1_1; -.
DR InParanoid; Q9SYM4; -.
DR OMA; REASIVW; -.
DR OrthoDB; 772297at2759; -.
DR PhylomeDB; Q9SYM4; -.
DR BRENDA; 2.4.1.15; 399.
DR PRO; PR:Q9SYM4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYM4; baseline and differential.
DR Genevisible; Q9SYM4; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IGI:TAIR.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0080186; P:developmental vegetative growth; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0048574; P:long-day photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0009832; P:plant-type cell wall biogenesis; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0010182; P:sugar mediated signaling pathway; IMP:TAIR.
DR GO; GO:0005992; P:trehalose biosynthetic process; IBA:GO_Central.
DR GO; GO:0005991; P:trehalose metabolic process; TAS:TAIR.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IBA:GO_Central.
DR CDD; cd03788; GT20_TPS; 1.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR012766; Trehalose_OtsA.
DR InterPro; IPR003337; Trehalose_PPase.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR Pfam; PF02358; Trehalose_PPase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02400; trehalose_OtsA; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cytoplasm; Glycosyltransferase; Reference proteome; Secreted;
KW Transferase; Vacuole.
FT CHAIN 1..942
FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT forming] 1"
FT /id="PRO_0000324822"
FT REGION 28..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..559
FT /note="Glycosyltransferase"
FT REGION 815..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 17
FT /note="R->Q: 3-fold increase in activity."
FT /evidence="ECO:0000269|PubMed:11978181"
FT MUTAGEN 27
FT /note="L->P: 4-fold increase in activity."
FT /evidence="ECO:0000269|PubMed:11978181"
FT CONFLICT 105
FT /note="A -> P (in Ref. 1; CAA69879)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="I -> K (in Ref. 1; CAA69879)"
FT /evidence="ECO:0000305"
FT CONFLICT 359..360
FT /note="AG -> TD (in Ref. 1; CAA69879)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="Q -> K (in Ref. 1; CAA69879)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="T -> P (in Ref. 1; CAA69879)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="K -> T (in Ref. 1; CAA69879)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="N -> I (in Ref. 1; CAA69879)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="F -> L (in Ref. 1; CAA69879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 942 AA; 105976 MW; B22AC11EA34CDDDB CRC64;
MPGNKYNCSS SHIPLSRTER LLRDRELREK RKSNRARNPN DVAGSSENSE NDLRLEGDSS
RQYVEQYLEG AAAAMAHDDA CERQEVRPYN RQRLLVVANR LPVSAVRRGE DSWSLEISAG
GLVSALLGVK EFEARWIGWA GVNVPDEVGQ KALSKALAEK RCIPVFLDEE IVHQYYNGYC
NNILWPLFHY LGLPQEDRLA TTRSFQSQFA AYKKANQMFA DVVNEHYEEG DVVWCHDYHL
MFLPKCLKEY NSKMKVGWFL HTPFPSSEIH RTLPSRSELL RSVLAADLVG FHTYDYARHF
VSACTRILGL EGTPEGVEDQ GRLTRVAAFP IGIDSDRFIR ALEVPEVIQH MKELKERFAG
RKVMLGVDRL DMIKGIPQKI LAFEKFLEEN ANWRDKVVLL QIAVPTRTDV PEYQKLTSQV
HEIVGRINGR FGTLTAVPIH HLDRSLDFHA LCALYAVTDV ALVTSLRDGM NLVSYEFVAC
QEAKKGVLIL SEFAGAAQSL GAGAILVNPW NITEVAASIG QALNMTAEER EKRHRHNFHH
VKTHTAQEWA ETFVSELNDT VIEAQLRISK VPPELPQHDA IQRYSKSNNR LLILGFNATL
TEPVDNQGRR GDQIKEMDLN LHPELKGPLK ALCSDPSTTI VVLSGSSRSV LDKNFGEYDM
WLAAENGMFL RLTNGEWMTT MPEHLNMEWV DSVKHVFKYF TERTPRSHFE TRDTSLIWNY
KYADIEFGRL QARDLLQHLW TGPISNASVD VVQGSRSVEV RAVGVTKGAA IDRILGEIVH
SKSMTTPIDY VLCIGHFLGK DEDVYTFFEP ELPSDMPAIA RSRPSSDSGA KSSSGDRRPP
SKSTHNNNKS GSKSSSSSNS NNNNKSSQRS LQSERKSGSN HSLGNSRRPS PEKISWNVLD
LKGENYFSCA VGRTRTNARY LLGSPDDVVC FLEKLADTTS SP
