TPS6_ARATH
ID TPS6_ARATH Reviewed; 860 AA.
AC Q94AH8; Q9C9W6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 6 {ECO:0000303|PubMed:16771775};
DE EC=2.4.1.15 {ECO:0000269|PubMed:17981987};
DE AltName: Full=Trehalose-6-phosphate synthase 6 {ECO:0000303|PubMed:16771775};
DE Short=AtTPS6 {ECO:0000303|PubMed:16771775};
GN Name=TPS6 {ECO:0000303|PubMed:16771775};
GN OrderedLocusNames=At1g68020 {ECO:0000312|Araport:AT1G68020};
GN ORFNames=T23K23.13 {ECO:0000312|EMBL:AAG52003.1};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM2).
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 [4]
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 [5]
RP PHOSPHORYLATION, INTERACTION WITH GRF/14-3-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16771775; DOI=10.1111/j.1365-313x.2006.02780.x;
RA Harthill J.E., Meek S.E.M., Morrice N., Peggie M.W., Borch J., Wong B.H.C.,
RA Mackintosh C.;
RT "Phosphorylation and 14-3-3 binding of Arabidopsis trehalose-phosphate
RT synthase 5 in response to 2-deoxyglucose.";
RL Plant J. 47:211-223(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ARG-152.
RX PubMed=17981987; DOI=10.1104/pp.107.107441;
RA Chary S.N., Hicks G.R., Choi Y.G., Carter D., Raikhel N.V.;
RT "Trehalose-6-phosphate synthase/phosphatase regulates cell shape and plant
RT architecture in Arabidopsis.";
RL Plant Physiol. 146:97-107(2008).
CC -!- FUNCTION: Regulates plant architecture, shape of epidermal pavement
CC cells and branching of trichomes. {ECO:0000269|PubMed:17981987}.
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:17981987};
CC -!- SUBUNIT: Binds to the phosphopeptide-binding site of GRF/14-3-3.
CC {ECO:0000269|PubMed:16771775}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94AH8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94AH8-2; Sequence=VSP_032376, VSP_032377;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, stems, flowers,
CC siliques and roots. {ECO:0000269|PubMed:17981987}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:16771775}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52003.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC012563; AAG52003.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34737.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34738.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60163.1; -; Genomic_DNA.
DR EMBL; AY046028; AAK76702.1; -; mRNA.
DR PIR; C96703; C96703.
DR RefSeq; NP_001322467.1; NM_001334340.1. [Q94AH8-1]
DR RefSeq; NP_564918.1; NM_105472.3. [Q94AH8-2]
DR RefSeq; NP_974105.1; NM_202376.3. [Q94AH8-1]
DR AlphaFoldDB; Q94AH8; -.
DR SMR; Q94AH8; -.
DR BioGRID; 28351; 1.
DR STRING; 3702.AT1G68020.2; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR iPTMnet; Q94AH8; -.
DR PaxDb; Q94AH8; -.
DR PRIDE; Q94AH8; -.
DR ProteomicsDB; 228384; -. [Q94AH8-1]
DR EnsemblPlants; AT1G68020.1; AT1G68020.1; AT1G68020. [Q94AH8-2]
DR EnsemblPlants; AT1G68020.2; AT1G68020.2; AT1G68020. [Q94AH8-1]
DR EnsemblPlants; AT1G68020.3; AT1G68020.3; AT1G68020. [Q94AH8-1]
DR GeneID; 843130; -.
DR Gramene; AT1G68020.1; AT1G68020.1; AT1G68020. [Q94AH8-2]
DR Gramene; AT1G68020.2; AT1G68020.2; AT1G68020. [Q94AH8-1]
DR Gramene; AT1G68020.3; AT1G68020.3; AT1G68020. [Q94AH8-1]
DR KEGG; ath:AT1G68020; -.
DR Araport; AT1G68020; -.
DR TAIR; locus:2200216; AT1G68020.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_3_1_1; -.
DR InParanoid; Q94AH8; -.
DR OMA; IFNWDEN; -.
DR OrthoDB; 772297at2759; -.
DR PhylomeDB; Q94AH8; -.
DR BRENDA; 2.4.1.15; 399.
DR PRO; PR:Q94AH8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94AH8; baseline and differential.
DR Genevisible; Q94AH8; AT.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IGI:TAIR.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IGI:TAIR.
DR GO; GO:0005992; P:trehalose biosynthetic process; IGI:TAIR.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IBA:GO_Central.
DR CDD; cd03788; GT20_TPS; 1.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
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; TIGR01484; HAD-SF-IIB; 1.
DR TIGRFAMs; TIGR00685; T6PP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycosyltransferase; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..860
FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT forming] 6"
FT /id="PRO_0000324827"
FT REGION 53..557
FT /note="Glycosyltransferase"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O23617"
FT VAR_SEQ 675..700
FT /note="LRKAVEWENCVAAVDCSWKQIAEPVM -> YSTKTFYFLALPLYLITQAPSN
FT YYTG (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_032376"
FT VAR_SEQ 701..860
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_032377"
FT MUTAGEN 152
FT /note="R->S: In cps-1; loss of pavement cell lobes and
FT altered trichomes branching."
FT /evidence="ECO:0000269|PubMed:17981987"
SQ SEQUENCE 860 AA; 97703 MW; A155BEB4EDAFD3A9 CRC64;
MVSRSYSNLL ELASGDSPTF GRMNRQIPRI MAVAGIMSNI DNDSKDTDLS PKDRIIIVAN
ELPIRAQRRV DGNGSGSSSS STCCSKGWNF SWDENSLLLQ LKDGLGDEAI EVIYVGCLKE
EIPLNEQEEV YQILLESFKC VPTFLPLDLY TRYYHGFCKQ QLWPLFHYML PLSPDLGGRF
DRTLWQAYVS VNKIFADRIM EVINPEDDFV WIHDYHLMVL PTFLRKRFNR VKLGFFLHSP
FPSSEIYKTL PIREELLRAL LNSDLIGFHT FDYARHFLSC CSRMLGLTYE SKRGYIGLEY
YGRTVSIKIL PVGIHMGQLQ SVLSLPETER KVGELIERYG RKGRTMLLGV DDMDIFKGIT
LKLLAMEQLL MQHPEWQGKV VLVQIANPAR GKGKDVKEMQ AETYSTVKRI NETFGRPGYD
PIVLIDAPLK FYERVAYYVV AECCLVTAVR DGMNLIPYEY IVSRQGNEKL DKILKLEANN
RNKKSMLVVS EFIGCSPSLS GAIRVNPWNV DAVADAMDSA LEVAEPEKQL RHEKHYKYVS
THDVGYWARS FLQDLERSCG EHGRRRCWGI GFGLSFRVVA LDQSFRKLSM EHIVSAYKRT
KTRAILLDYD DTLMPQGSID KRPSSKSIDI LNTLCRDKGN LVFIVSAKSR ETLSDWFSPC
EKLGIAAEHG YFLRLRKAVE WENCVAAVDC SWKQIAEPVM ELYTETTDGS TIEDKETALV
WSYEDADPDF GSCQAKELLD HLESVLANEP VTVKRGQNYV EVKPQGVSKG LIARRMLSMM
QERGTLPEFV LCIGDDRSDE DMFEVICSST EGPSIAPRAE IFACTVGQKP SKAKYYLDDT
TEIVRLMHGL ASVTDQITPV
