TPPG_ARATH
ID TPPG_ARATH Reviewed; 377 AA.
AC Q9SUW0;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable trehalose-phosphate phosphatase G;
DE Short=AtTPPG;
DE EC=3.1.3.12;
DE AltName: Full=Trehalose 6-phosphate phosphatase;
DE AltName: Full=Trehalose-phosphate phosphatase 6;
GN Name=TPPG; Synonyms=TPP6; OrderedLocusNames=At4g22590; ORFNames=F7K2.170;
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL033545; CAA22164.1; -; Genomic_DNA.
DR EMBL; AL161557; CAB79214.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84627.1; -; Genomic_DNA.
DR EMBL; AK221933; BAD94370.1; -; mRNA.
DR EMBL; AK316702; BAH19429.1; -; mRNA.
DR PIR; T05453; T05453.
DR RefSeq; NP_193990.1; NM_118385.4.
DR AlphaFoldDB; Q9SUW0; -.
DR SMR; Q9SUW0; -.
DR STRING; 3702.AT4G22590.1; -.
DR iPTMnet; Q9SUW0; -.
DR PaxDb; Q9SUW0; -.
DR PRIDE; Q9SUW0; -.
DR ProteomicsDB; 245253; -.
DR EnsemblPlants; AT4G22590.1; AT4G22590.1; AT4G22590.
DR GeneID; 828355; -.
DR Gramene; AT4G22590.1; AT4G22590.1; AT4G22590.
DR KEGG; ath:AT4G22590; -.
DR Araport; AT4G22590; -.
DR TAIR; locus:2127510; AT4G22590.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_037265_1_0_1; -.
DR InParanoid; Q9SUW0; -.
DR OMA; MGSYANG; -.
DR OrthoDB; 974358at2759; -.
DR PhylomeDB; Q9SUW0; -.
DR UniPathway; UPA00299; -.
DR PRO; PR:Q9SUW0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUW0; baseline and differential.
DR Genevisible; Q9SUW0; 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..377
FT /note="Probable trehalose-phosphate phosphatase G"
FT /id="PRO_0000417649"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 377 AA; 42634 MW; 80A23F29221A8FA4 CRC64;
MDLNINKTTP VLSDPTTPVS KTRLGSSFPS GRFMMNSRKK IPKLDDVRSN GWLDAMISSS
PPRKRLVKDF NIEIAPEDDF SQRAWMLKYP SAITSFAHIA AQAKNKKIAV FLDYDGTLSP
IVDDPDRAIM SDAMRAAVKD VAKYFPTAII SGRSRDKVYQ LVGLTELYYA GSHGMDIMTP
VNPNGSPEDP NCIKTTDQQG EEVNLFQPAK EFIPVIEEVY NNLVEITKCI KGAKVENHKF
CTSVHYRNVD EKDWPLVAQR VHDHLKRYPR LRITHGRKVL EVRPVIEWNK GKAVEFLLES
LGLSNNDEFL PIFIGDDKTD EDAFKVLREG NRGFGILVSS VPKESNAFYS LRDPSEVKKF
LKTLVKWGKM ESSKTSF
