TPS11_ARATH
ID TPS11_ARATH Reviewed; 862 AA.
AC Q9ZV48; Q94B44;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable alpha,alpha-trehalose-phosphate synthase [UDP-forming] 11;
DE EC=2.4.1.15;
DE AltName: Full=Trehalose-6-phosphate synthase 11;
DE Short=AtTPS11;
GN Name=TPS11; Synonyms=TPSB; OrderedLocusNames=At2g18700; ORFNames=MSF3.8;
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], AND TISSUE SPECIFICITY.
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 [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] OF 588-778 (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 589-862 (ISOFORM 2).
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 [6]
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ZV48-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZV48-2; Sequence=VSP_032378;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, stems and flowers.
CC {ECO:0000269|PubMed:11520870}.
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=AAK68805.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC005724; AAD08939.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06795.1; -; Genomic_DNA.
DR EMBL; AV822913; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY042865; AAK68805.1; ALT_INIT; mRNA.
DR EMBL; AY081537; AAM10099.1; -; mRNA.
DR PIR; E84567; E84567.
DR RefSeq; NP_179460.1; NM_127426.3. [Q9ZV48-1]
DR AlphaFoldDB; Q9ZV48; -.
DR SMR; Q9ZV48; -.
DR BioGRID; 1742; 1.
DR STRING; 3702.AT2G18700.1; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR PaxDb; Q9ZV48; -.
DR PRIDE; Q9ZV48; -.
DR ProteomicsDB; 228328; -. [Q9ZV48-1]
DR EnsemblPlants; AT2G18700.1; AT2G18700.1; AT2G18700. [Q9ZV48-1]
DR GeneID; 816385; -.
DR Gramene; AT2G18700.1; AT2G18700.1; AT2G18700. [Q9ZV48-1]
DR KEGG; ath:AT2G18700; -.
DR Araport; AT2G18700; -.
DR TAIR; locus:2054027; AT2G18700.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_3_1_1; -.
DR InParanoid; Q9ZV48; -.
DR OMA; DSVCRDG; -.
DR OrthoDB; 772297at2759; -.
DR PhylomeDB; Q9ZV48; -.
DR PRO; PR:Q9ZV48; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZV48; baseline and differential.
DR Genevisible; Q9ZV48; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005992; P:trehalose biosynthetic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Glycosyltransferase; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..862
FT /note="Probable alpha,alpha-trehalose-phosphate synthase
FT [UDP-forming] 11"
FT /id="PRO_0000324832"
FT REGION 50..538
FT /note="Glycosyltransferase"
FT REGION 838..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O23617"
FT VAR_SEQ 654
FT /note="T -> TRYFAKTLPFHHLPSHFCKVNTFLLLICNH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074,
FT ECO:0000303|PubMed:14593172"
FT /id="VSP_032378"
SQ SEQUENCE 862 AA; 98275 MW; 2D2808FBFA1D5B6A CRC64;
MSPESWKDQL SLVSADDYRI MGRNRIPNAV TKLSGLETDD PNGGAWVTKP KRIVVSNQLP
LRAHRDISSN KWCFEFDNDS LYLQLKDGFP PETEVVYVGS LNADVLPSEQ EDVSQFLLEK
FQCVPTFLPS DLLNKYYHGF CKHYLWPIFH YLLPMTQAQG SLFDRSNWRA YTTVNKIFAD
KIFEVLNPDD DYVWIHDYHL MILPTFLRNR FHRIKLGIFL HSPFPSSEIY RTLPVRDEIL
KGFLNCDLVG FHTFDYARHF LSCCSRMLGL DYESKRGYIG LEYFGRTVSI KILPVGIHMG
QIESIKASEK TAEKVKRLRE RFKGNIVMLG VDDLDMFKGI SLKFWAMGQL LEQNEELRGK
VVLVQITNPA RSSGKDVQDV EKQINLIADE INSKFGRPGG YKPIVFINGP VSTLDKVAYY
AISECVVVNA VRDGMNLVPY KYTVTRQGSP ALDAALGFGE DDVRKSVIIV SEFIGCSPSL
SGAIRVNPWN IDAVTNAMSS AMTMSDKEKN LRHQKHHKYI SSHNVAYWAR SYDQDLQRAC
KDHYNKRFWG VGFGLFFKVV ALDPNFRRLC GETIVPAYRR SSSRLILLDY DGTMMDQDTL
DKRPSDDLIS LLNRLCDDPS NLVFIVSGRG KDPLSKWFDS CPNLGISAEH GYFTRWNSNS
PWETSELPAD LSWKKIAKPV MNHYMEATDG SFIEEKESAM VWHHQEADHS FGSWQAKELL
DHLESVLTNE PVVVKRGQHI VEVKPQGVSK GKVVEHLIAT MRNTKGKRPD FLLCIGDDRS
DEDMFDSIVK HQDVSSIGLE EVFACTVGQK PSKAKYYLDD TPSVIKMLEW LASASDGSKH
EQQKKQSKFT FQQPMGQCRK KA
