TPPH_ARATH
ID TPPH_ARATH Reviewed; 349 AA.
AC Q8GWG2; O65664;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Probable trehalose-phosphate phosphatase H;
DE Short=AtTPPH;
DE EC=3.1.3.12;
DE AltName: Full=Trehalose 6-phosphate phosphatase;
GN Name=TPPH; OrderedLocusNames=At4g39770; ORFNames=T19P19.160;
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=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 [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 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 [6]
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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18763.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80640.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022605; CAA18763.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161595; CAB80640.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE87117.1; -; Genomic_DNA.
DR EMBL; AK118867; BAC43453.1; -; mRNA.
DR EMBL; BT005555; AAO63975.1; -; mRNA.
DR PIR; T05014; T05014.
DR RefSeq; NP_195687.2; NM_120140.3.
DR AlphaFoldDB; Q8GWG2; -.
DR SMR; Q8GWG2; -.
DR STRING; 3702.AT4G39770.1; -.
DR PaxDb; Q8GWG2; -.
DR PRIDE; Q8GWG2; -.
DR EnsemblPlants; AT4G39770.1; AT4G39770.1; AT4G39770.
DR GeneID; 830135; -.
DR Gramene; AT4G39770.1; AT4G39770.1; AT4G39770.
DR KEGG; ath:AT4G39770; -.
DR Araport; AT4G39770; -.
DR TAIR; locus:2135272; AT4G39770.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_037265_1_1_1; -.
DR InParanoid; Q8GWG2; -.
DR OMA; HKLAKHP; -.
DR OrthoDB; 974358at2759; -.
DR PhylomeDB; Q8GWG2; -.
DR UniPathway; UPA00299; -.
DR PRO; PR:Q8GWG2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GWG2; baseline and differential.
DR Genevisible; Q8GWG2; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IDA:TAIR.
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..349
FT /note="Probable trehalose-phosphate phosphatase H"
FT /id="PRO_0000417650"
SQ SEQUENCE 349 AA; 39999 MW; B726745341DDE36F CRC64;
MVRFIEENTK LVEKETGNKS NNDVTTTKKK ALQDIIINNG VGLINSWVDS MRACSPTHLK
SLLKQSSWLT EHPSALDMFE EILHLSEGKQ IVMFLDYDGT LSPIVDDPDR AFMSRKMRRT
VRKLANCFPT AIVSGRCIEK VYNFVKLTEL YYAGSHGMDI KGPEQGSKYE QILQDSKSLL
CQPATEFLPM IDEVYHKLVE KTKSTPGAQV ENNKFCVSVH FRRVDENNWS DLANQVRSVM
KDYPKLRLTQ GRKVLEVRPI IKWDKGKALE FLLESLGYAN CTDVFPLYIG DDRTDEDAFK
VLRERRQGLG ILVSKFPKET SASYSLQEPD EVMEFLQRLV EWKQLRSGA