TPPF_ARATH
ID TPPF_ARATH Reviewed; 368 AA.
AC Q9SU39;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable trehalose-phosphate phosphatase F;
DE Short=AtTPPF;
DE EC=3.1.3.12;
DE AltName: Full=Trehalose 6-phosphate phosphatase;
DE AltName: Full=Trehalose-phosphate phosphatase 5;
GN Name=TPPF; Synonyms=TPP5; OrderedLocusNames=At4g12430; ORFNames=T1P17.20;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
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.
RX PubMed=12508064; DOI=10.1093/jxb/erg039;
RA Eastmond P.J., Li Y., Graham I.A.;
RT "Is trehalose-6-phosphate a regulator of sugar metabolism in plants?";
RL J. Exp. Bot. 54:533-537(2003).
RN [5]
RP INDUCTION, AND NOMENCLATURE.
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).
CC -!- FUNCTION: Removes the phosphate from trehalose 6-phosphate to produce
CC free trehalose. Trehalose accumulation in plant may improve abiotic
CC stress tolerance (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Participates in the regulation of trehalose metabolism.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-
CC trehalose + phosphate; Xref=Rhea:RHEA:23420, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:43474, ChEBI:CHEBI:58429; EC=3.1.3.12;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC -!- INDUCTION: By trehalose. {ECO:0000269|PubMed:15181209}.
CC -!- SIMILARITY: Belongs to the trehalose phosphatase family. {ECO:0000305}.
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DR EMBL; AL049730; CAB41713.1; -; Genomic_DNA.
DR EMBL; AL161534; CAB78286.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83130.1; -; Genomic_DNA.
DR EMBL; AY059840; AAL24322.1; -; mRNA.
DR EMBL; BT002566; AAO00926.1; -; mRNA.
DR PIR; T07635; T07635.
DR RefSeq; NP_192980.1; NM_117313.2.
DR AlphaFoldDB; Q9SU39; -.
DR SMR; Q9SU39; -.
DR STRING; 3702.AT4G12430.1; -.
DR PaxDb; Q9SU39; -.
DR PRIDE; Q9SU39; -.
DR ProteomicsDB; 228409; -.
DR EnsemblPlants; AT4G12430.1; AT4G12430.1; AT4G12430.
DR GeneID; 826855; -.
DR Gramene; AT4G12430.1; AT4G12430.1; AT4G12430.
DR KEGG; ath:AT4G12430; -.
DR Araport; AT4G12430; -.
DR TAIR; locus:2135540; AT4G12430.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_037265_1_1_1; -.
DR InParanoid; Q9SU39; -.
DR OMA; IIAQRVH; -.
DR OrthoDB; 974358at2759; -.
DR PhylomeDB; Q9SU39; -.
DR UniPathway; UPA00299; -.
DR PRO; PR:Q9SU39; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SU39; baseline and differential.
DR Genevisible; Q9SU39; AT.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IBA:GO_Central.
DR GO; GO:0005992; P:trehalose biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR044651; OTSB-like.
DR InterPro; IPR003337; Trehalose_PPase.
DR PANTHER; PTHR43768; PTHR43768; 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 Hydrolase; Reference proteome; Stress response.
FT CHAIN 1..368
FT /note="Probable trehalose-phosphate phosphatase F"
FT /id="PRO_0000417648"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 41608 MW; 166FB1370FE59A54 CRC64;
MDLNSNHKSS VLKDPSPSVN QSRLGVSSRF MMSQWKKPAK LDDVRSNGWL DAMISSSPPR
KKLVKDFNVE VAPEDDFAQR AWMVKYPSAI SSFAHIAAQA KKKKIAVFLD YDGTLSPIVD
DPDRAIMSDA MRSAVKDVAS YFPTAIISGR SRDKVYQLVG LTELYYAGSH GMDIMTSSDG
PNCFKSTDQQ GKEVNLFQPA REFIPVIDEV FRTLVEKMKD IKGAKVENHK FCASVHYRNV
DEKDWPIIAQ RVHDHLKQYP RLRLTHGRKV LEVRPVIDWN KGRAVEFLLE SLGLSNKDDL
LPIYIGDDTT DEDAFKVLRD GNRGFGILVS SIPKESNAFY SLRDPSEVKK FLKTLVKWAK
LEKNSTGF
