TPP1_ORYSJ
ID TPP1_ORYSJ Reviewed; 371 AA.
AC Q75WV3; A0A0P0VMN9;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Probable trehalose-phosphate phosphatase 1;
DE Short=OsTPP1;
DE EC=3.1.3.12;
DE AltName: Full=Trehalose 6-phosphate phosphatase;
GN Name=TPP1; OrderedLocusNames=Os02g0661100, LOC_Os02g44230;
GN ORFNames=OsJ_07820, P0516F12.9, P0708H12.35;
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, INDUCTION, GENE
RP 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).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND INDUCTION.
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 [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=18365248; DOI=10.1007/s00425-008-0729-x;
RA Ge L.F., Chao D.Y., Shi M., Zhu M.Z., Gao J.P., Lin H.X.;
RT "Overexpression of the trehalose-6-phosphate phosphatase gene OsTPP1
RT confers stress tolerance in rice and results in the activation of stress
RT responsive genes.";
RL Planta 228:191-201(2008).
CC -!- FUNCTION: Removes the phosphate from trehalose 6-phosphate to produce
CC free trehalose. Trehalose accumulation in plant improves abiotic stress
CC tolerance. {ECO:0000269|PubMed:16240171, ECO:0000269|PubMed:17257172,
CC ECO:0000269|PubMed:18365248}.
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:16240171, 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=92.1 uM for trehalose 6-phosphate {ECO:0000269|PubMed:17257172};
CC pH dependence:
CC Optimum pH is 6.5-7.0. {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:16240171, ECO:0000269|PubMed:17257172,
CC ECO:0000269|PubMed:18365248}.
CC -!- MISCELLANEOUS: Over-expression of TPP1 increases trehalose levels and
CC enhances tolerance to salt and cold stresses.
CC {ECO:0000305|PubMed:18365248}.
CC -!- SIMILARITY: Belongs to the trehalose phosphatase family. {ECO:0000305}.
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DR EMBL; AB120515; BAD12596.1; -; mRNA.
DR EMBL; AP004883; BAD25622.1; -; Genomic_DNA.
DR EMBL; AP005072; BAD25753.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09559.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS80139.1; -; Genomic_DNA.
DR EMBL; CM000139; EEE57517.1; -; Genomic_DNA.
DR EMBL; AK103391; BAG96056.1; -; mRNA.
DR RefSeq; XP_015623255.1; XM_015767769.1.
DR AlphaFoldDB; Q75WV3; -.
DR SMR; Q75WV3; -.
DR STRING; 4530.OS02T0661100-01; -.
DR PaxDb; Q75WV3; -.
DR EnsemblPlants; Os02t0661100-01; Os02t0661100-01; Os02g0661100.
DR GeneID; 4330221; -.
DR Gramene; Os02t0661100-01; Os02t0661100-01; Os02g0661100.
DR KEGG; osa:4330221; -.
DR eggNOG; KOG1050; Eukaryota.
DR InParanoid; Q75WV3; -.
DR OMA; SSANHEH; -.
DR OrthoDB; 974358at2759; -.
DR BRENDA; 3.1.3.12; 4460.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q75WV3; baseline and differential.
DR Genevisible; Q75WV3; OS.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IGI:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IGI: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..371
FT /note="Probable trehalose-phosphate phosphatase 1"
FT /id="PRO_0000417653"
SQ SEQUENCE 371 AA; 41128 MW; 9F518916127CCD34 CRC64;
MDLSNSSPVI TDPVAISQQL LGGLPSNLMQ FSVMPGGYSS SGMNVGVSRL KIEEVLVNGL
LDAMKSSSPR RRLNVAFGED NSSEEEDPAY SAWMAKCPSA LASFKQIVAS AQGKKIAVFL
DYDGTLSPIV DDPDKAVMSP VMRAAVRNVA KYFPTAIVSG RSRNKVFEFV KLKELYYAGS
HGMDIMAPSA NHEHSAEKSK QANLFQPAHD FLPMIDEVTK SLLQVVSGIE GATVENNKFC
VSVHYRNVAE KDWKLVARLV NEVLEAFPRL KVTNGRMVLE VRPVIDWDKG KAVEFLLQSL
GLNDSENVIP IYIGDDRTDE DAFKVLRQRN CGYGILVSQV PKETEAFYSL RDPSEVMEFL
NFLVRWKKHS V
