TALDO_RAT
ID TALDO_RAT Reviewed; 337 AA.
AC Q9EQS0; Q6PCV1;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Transaldolase {ECO:0000250|UniProtKB:P37837};
DE EC=2.2.1.2;
GN Name=Taldo1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Perl A., Bachand G.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 72-81; 103-121; 125-130; 220-225; 246-265; 270-277 AND
RP 315-321, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalyzes the rate-limiting step of the non-oxidative phase
CC in the pentose phosphate pathway. Catalyzes the reversible conversion
CC of sedheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into
CC erythrose-4-phosphate and beta-D-fructose 6-phosphate.
CC {ECO:0000250|UniProtKB:Q93092}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC beta-D-fructose 6-phosphate + D-erythrose 4-phosphate;
CC Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897, ChEBI:CHEBI:57483,
CC ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; EC=2.2.1.2;
CC Evidence={ECO:0000250|UniProtKB:P37837};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17054;
CC Evidence={ECO:0000250|UniProtKB:P37837};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17055;
CC Evidence={ECO:0000250|UniProtKB:P37837};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-
CC ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage):
CC step 2/3. {ECO:0000250|UniProtKB:Q93092}.
CC -!- SUBUNIT: Homodimer. Interacts with KPNA1 and KPNA4.
CC {ECO:0000250|UniProtKB:Q93092}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q93092}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q93092}. Note=Shuttles between the nucleus and
CC the cytoplasm. Actively transported into the nucleus in an importin
CC alpha/beta-dependent manner. Exported into the cytoplasm by CRM1.
CC {ECO:0000250|UniProtKB:Q93092}.
CC -!- DOMAIN: The first 10 amino acids are essential for nuclear
CC localization. {ECO:0000250|UniProtKB:Q93092}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF069306; AAG43169.1; -; mRNA.
DR EMBL; BC059126; AAH59126.1; -; mRNA.
DR RefSeq; NP_113999.2; NM_031811.3.
DR AlphaFoldDB; Q9EQS0; -.
DR SMR; Q9EQS0; -.
DR BioGRID; 249806; 2.
DR IntAct; Q9EQS0; 1.
DR STRING; 10116.ENSRNOP00000024863; -.
DR iPTMnet; Q9EQS0; -.
DR PhosphoSitePlus; Q9EQS0; -.
DR World-2DPAGE; 0004:Q9EQS0; -.
DR jPOST; Q9EQS0; -.
DR PaxDb; Q9EQS0; -.
DR PRIDE; Q9EQS0; -.
DR Ensembl; ENSRNOT00000024863; ENSRNOP00000024863; ENSRNOG00000018367.
DR GeneID; 83688; -.
DR KEGG; rno:83688; -.
DR UCSC; RGD:620674; rat.
DR CTD; 6888; -.
DR RGD; 620674; Taldo1.
DR eggNOG; KOG2772; Eukaryota.
DR GeneTree; ENSGT00390000017361; -.
DR HOGENOM; CLU_047470_0_1_1; -.
DR InParanoid; Q9EQS0; -.
DR OMA; KFGYKTL; -.
DR OrthoDB; 1402459at2759; -.
DR PhylomeDB; Q9EQS0; -.
DR TreeFam; TF300757; -.
DR Reactome; R-RNO-163754; Insulin effects increased synthesis of Xylulose-5-Phosphate.
DR Reactome; R-RNO-71336; Pentose phosphate pathway.
DR UniPathway; UPA00115; UER00414.
DR PRO; PR:Q9EQS0; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018367; Expressed in jejunum and 20 other tissues.
DR Genevisible; Q9EQS0; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IDA:RGD.
DR GO; GO:0048029; F:monosaccharide binding; IDA:RGD.
DR GO; GO:0004801; F:transaldolase activity; IDA:RGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IDA:RGD.
DR GO; GO:0019682; P:glyceraldehyde-3-phosphate metabolic process; IDA:RGD.
DR GO; GO:0006098; P:pentose-phosphate shunt; IDA:RGD.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IDA:RGD.
DR CDD; cd00957; Transaldolase_TalAB; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00492; Transaldolase_1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR004730; Transaldolase_1.
DR InterPro; IPR018225; Transaldolase_AS.
DR PANTHER; PTHR10683; PTHR10683; 1.
DR PANTHER; PTHR10683:SF18; PTHR10683:SF18; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR TIGRFAMs; TIGR00874; talAB; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Nucleus; Pentose shunt;
KW Phosphoprotein; Reference proteome; Schiff base; Transferase.
FT CHAIN 1..337
FT /note="Transaldolase"
FT /id="PRO_0000173567"
FT MOTIF 1..10
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q93092"
FT ACT_SITE 142
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250|UniProtKB:P37837"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q93092"
FT MOD_RES 219
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P37837"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P37837"
FT MOD_RES 269
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P37837"
FT MOD_RES 286
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P37837"
FT MOD_RES 321
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P37837"
FT CONFLICT 100
FT /note="P -> L (in Ref. 1; AAG43169)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 37460 MW; F01F64276053B45D CRC64;
MSGSPVKRQR MESALDQLKQ FTTVVADTGD FNAIDEYKPQ DATTNPSLIL AAAQMPAYQE
LVEEAIAYGK KLGGPQEEQI KNAIDKLFVL FGAEILKKIP GRVSTEVDAR LSFDKDAMVA
RARRIIELYK EAGISKDRIL IKLSSTWEGI QAGKELEEQH GIHCNMTLLF SFAQAVACAE
AGVTLISPFV GRILDWHVAN TDKKSYEPQE DPGVKSVTKI YNYYKKFGYK TIVMGASFRN
TGEIKALAGC DFLTISPKLL GELLKDSSKL APTLSVKAAQ TSDLEKIHLD EKAFRWLHNE
DQMAVEKLSD GIRKFAADAI KLERMLTERM FSAENGK
