TPRA3_MAIZE
ID TPRA3_MAIZE Reviewed; 361 AA.
AC Q1W5S8;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Trehalose 6-phosphate phosphatase RA3 {ECO:0000305};
DE EC=3.1.3.12 {ECO:0000269|PubMed:16688177};
DE AltName: Full=Protein RAMOSA 3 {ECO:0000303|PubMed:16688177};
GN Name=RA3 {ECO:0000303|PubMed:16688177};
GN ORFNames=ZEAMMB73_Zm00001d022193 {ECO:0000312|EMBL:ONM59832.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16688177; DOI=10.1038/nature04725;
RA Satoh-Nagasawa N., Nagasawa N., Malcomber S.T., Sakai H., Jackson D.;
RT "A trehalose metabolic enzyme controls inflorescence architecture in
RT maize.";
RL Nature 441:227-230(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
CC -!- FUNCTION: Removes the phosphate from trehalose 6-phosphate to produce
CC free trehalose. Is specific for trehalose 6-phosphate. Does not possess
CC activity toward glucose, sucrose or fructose 6-phosphates. Regulates
CC inflorescence branching. Required to establish the correct identity and
CC determinacy of axillary meristems in both male and female
CC inflorescences. May act through a sugar signal that moves into axillary
CC meristems. Acts upstream of RA1. May have a transcriptional regulatory
CC function. {ECO:0000269|PubMed:16688177}.
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:16688177};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in axillary inflorescence meristems.
CC {ECO:0000269|PubMed:16688177}.
CC -!- DISRUPTION PHENOTYPE: Additional long branches in tassels and abnormal
CC long branches at their bases in ears. Abnormal identity of axillary
CC meristems. {ECO:0000269|PubMed:16688177}.
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; DQ436920; ABD92779.1; -; mRNA.
DR EMBL; BT036738; ACF81743.1; -; mRNA.
DR EMBL; CM007650; ONM59832.1; -; Genomic_DNA.
DR RefSeq; NP_001105864.1; NM_001112394.2.
DR AlphaFoldDB; Q1W5S8; -.
DR SMR; Q1W5S8; -.
DR STRING; 4577.GRMZM2G014729_P01; -.
DR PRIDE; Q1W5S8; -.
DR EnsemblPlants; Zm00001eb327910_T002; Zm00001eb327910_P002; Zm00001eb327910.
DR GeneID; 732774; -.
DR Gramene; Zm00001eb327910_T002; Zm00001eb327910_P002; Zm00001eb327910.
DR KEGG; zma:732774; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_037265_1_1_1; -.
DR OrthoDB; 974358at2759; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000007305; Chromosome 7.
DR ExpressionAtlas; Q1W5S8; baseline and differential.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:2000032; P:regulation of secondary shoot formation; IMP: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 Growth regulation; Hydrolase; Reference proteome.
FT CHAIN 1..361
FT /note="Trehalose 6-phosphate phosphatase RA3"
FT /id="PRO_0000442047"
SQ SEQUENCE 361 AA; 39773 MW; 3010168930E29941 CRC64;
MTKHAAYSSE DVVAAVAAPA PAGRHFTSFQ ALKGAPLDCK KHAAVDLSAS GAAVVGGGPW
FESMKASSPR RAADAEHGDW MEKHPSALAQ FEPLLAAAKG KQIVMFLDYD GTLSPIVEDP
DRAVMSEEMR EAVRRVAEHF PTAIVSGRCR DKVLNFVKLT ELYYAGSHGM DIQGPAACRQ
PNHVQQAEAA AVHYQAASEF LPVIEEVFRT LTAKMESIAG ARVEHNKYCL SVHFRCVREE
EWNAVNEEVR SVLREYPNLK LTHGRKVLEI RPSIKWDKGK ALEFLLKSLG YAGRNDVFPI
YIGDDRTDED AFKVLRNMGQ GIGILVSKLP KETAASYSLS DPAEVKEFLR KLANKKGARQ
P
