TPP2_ORYSJ
ID TPP2_ORYSJ Reviewed; 382 AA.
AC Q9FWQ2; A0A0P0XX17; Q7XCC1;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable trehalose-phosphate phosphatase 2;
DE Short=OsTPP2;
DE EC=3.1.3.12;
DE AltName: Full=Trehalose 6-phosphate phosphatase;
GN Name=TPP2; OrderedLocusNames=Os10g0553300, LOC_Os10g40550;
GN ORFNames=OSJNBa0015J15.3;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Yukihikari;
RX PubMed=17257172; DOI=10.1111/j.1742-4658.2007.05658.x;
RA Shima S., Matsui H., Tahara S., Imai R.;
RT "Biochemical characterization of rice trehalose-6-phosphate phosphatases
RT supports distinctive functions of these plant enzymes.";
RL FEBS J. 274:1192-1201(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Yukihikari;
RX PubMed=16240171; DOI=10.1007/s11103-005-7404-4;
RA Pramanik M.H., Imai R.;
RT "Functional identification of a trehalose 6-phosphate phosphatase gene that
RT is involved in transient induction of trehalose biosynthesis during
RT chilling stress in rice.";
RL Plant Mol. Biol. 58:751-762(2005).
CC -!- FUNCTION: Removes the phosphate from trehalose 6-phosphate to produce
CC free trehalose. Trehalose accumulation in plant may improve abiotic
CC stress tolerance. {ECO:0000269|PubMed:17257172}.
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 Evidence={ECO:0000269|PubMed:17257172};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=186 uM for trehalose 6-phosphate {ECO:0000269|PubMed:17257172};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:17257172};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC -!- TISSUE SPECIFICITY: Expressed in roots and shoots.
CC {ECO:0000269|PubMed:17257172}.
CC -!- INDUCTION: By cold, drought, salt stress and abscisic acid (ABA).
CC {ECO:0000269|PubMed:17257172}.
CC -!- SIMILARITY: Belongs to the trehalose phosphatase family. {ECO:0000305}.
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DR EMBL; AB277360; BAF34519.1; -; mRNA.
DR EMBL; AC026758; AAG13478.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP54952.1; -; Genomic_DNA.
DR EMBL; DP000086; ABB47970.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF27173.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT11974.1; -; Genomic_DNA.
DR RefSeq; XP_015612912.1; XM_015757426.1.
DR RefSeq; XP_015612914.1; XM_015757428.1.
DR RefSeq; XP_015612915.1; XM_015757429.1.
DR AlphaFoldDB; Q9FWQ2; -.
DR SMR; Q9FWQ2; -.
DR STRING; 4530.OS10T0553300-01; -.
DR PaxDb; Q9FWQ2; -.
DR PRIDE; Q9FWQ2; -.
DR EnsemblPlants; Os10t0553300-01; Os10t0553300-01; Os10g0553300.
DR GeneID; 4349333; -.
DR Gramene; Os10t0553300-01; Os10t0553300-01; Os10g0553300.
DR KEGG; osa:4349333; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_037265_1_0_1; -.
DR InParanoid; Q9FWQ2; -.
DR OMA; IIAQRVH; -.
DR OrthoDB; 974358at2759; -.
DR BRENDA; 3.1.3.12; 8948.
DR PlantReactome; R-OSA-1119516; Trehalose biosynthesis I.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR Genevisible; Q9FWQ2; OS.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0005992; P:trehalose biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Hydrolase; Reference proteome; Stress response.
FT CHAIN 1..382
FT /note="Probable trehalose-phosphate phosphatase 2"
FT /id="PRO_0000417654"
SQ SEQUENCE 382 AA; 42578 MW; 67940C5634E0773D CRC64;
MDLKTSNSPV IADPLPKLAL PSAVMTYTTP TSFPSTGLYL NTPKKKPLPG KIEEVRAAGW
LDLMLASSPP RKRQTKDFAN DVQADELDLL YRNWVVNHPS ALTSFEDIVN LARGKRLALF
LDYDGTLSPI VDNPENAVMS DEMRSAVKHV ASLFPTAIIS GRSRDKVFDF VKLTELYYAG
SHGMDIMGPV RKSDSSGQHV ECIRSTDSEG KEVNLFQPAS EFLPMISEVY KKLSESIKDI
DGARMEDNKF CVSVHYRNVA PHDYGEVHQR VTAVLKNYPC LRLTHGRKVL EVRPVIDWNK
GKAVEFLLES LGLCGKEDVL PIYVGDDKTD EDAFKVLKAN SIGFGILVSS VPKDTDAFYS
VRDPAEVMEF LKKLASWKEE ST
