TALDO_MOUSE
ID TALDO_MOUSE Reviewed; 337 AA.
AC Q93092; P70358; P70703; Q52KM4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Transaldolase;
DE EC=2.2.1.2 {ECO:0000269|PubMed:17003133, ECO:0000305|PubMed:27703206};
GN Name=Taldo1; Synonyms=Tal, Taldo;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9524206; DOI=10.1016/s0378-1119(97)00639-2;
RA Kusuda J., Hirai M., Toyoda A., Tanuma R., Nomura-Kitabayashi A.,
RA Hashimoto K.;
RT "Cloning and chromosomal localization of a paralog and a mouse homolog of
RT the human transaldolase gene.";
RL Gene 209:13-21(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary gland;
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 87-97 AND 259-265, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17003133; DOI=10.1073/pnas.0602678103;
RA Perl A., Qian Y., Chohan K.R., Shirley C.R., Amidon W., Banerjee S.,
RA Middleton F.A., Conkrite K.L., Barcza M., Gonchoroff N., Suarez S.S.,
RA Banki K.;
RT "Transaldolase is essential for maintenance of the mitochondrial
RT transmembrane potential and fertility of spermatozoa.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14813-14818(2006).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, AND PATHWAY.
RX PubMed=19436114; DOI=10.1172/jci35722;
RA Hanczko R., Fernandez D.R., Doherty E., Qian Y., Vas G., Niland B.,
RA Telarico T., Garba A., Banerjee S., Middleton F.A., Barrett D., Barcza M.,
RA Banki K., Landas S.K., Perl A.;
RT "Prevention of hepatocarcinogenesis and increased susceptibility to
RT acetaminophen-induced liver failure in transaldolase-deficient mice by N-
RT acetylcysteine.";
RL J. Clin. Invest. 119:1546-1557(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-115 AND LYS-321, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP ALTERNATIVE INITIATION, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF MET-1;
RP LYS-7; ARG-8; ARG-10 AND MET-11, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2),
RP INTERACTION WITH KPNA1 AND KPNA4 (ISOFORM 1), AND SUBUNIT.
RX PubMed=27703206; DOI=10.1038/srep34648;
RA Moriyama T., Tanaka S., Nakayama Y., Fukumoto M., Tsujimura K., Yamada K.,
RA Bamba T., Yoneda Y., Fukusaki E., Oka M.;
RT "Two isoforms of TALDO1 generated by alternative translational initiation
RT show differential nucleocytoplasmic distribution to regulate the global
RT metabolic network.";
RL Sci. Rep. 6:34648-34648(2016).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 13-337.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of mouse transaldolase.";
RL Submitted (DEC-2005) to the PDB data bank.
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 (PubMed:17003133,
CC PubMed:27703206). Not only acts as a pentose phosphate pathway enzyme,
CC but also affects other metabolite pathways by altering its subcellular
CC localization between the nucleus and the cytoplasm (PubMed:27703206).
CC {ECO:0000269|PubMed:17003133, ECO:0000269|PubMed:27703206}.
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:0000269|PubMed:17003133, ECO:0000305|PubMed:27703206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17054;
CC Evidence={ECO:0000305|PubMed:27703206};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17055;
CC Evidence={ECO:0000305|PubMed:27703206};
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:0000269|PubMed:19436114}.
CC -!- SUBUNIT: Homodimer (PubMed:27703206). Heterodimer with isoform 2
CC (PubMed:27703206). Interacts with KPNA1 and KPNA4 (PubMed:27703206).
CC {ECO:0000269|PubMed:27703206}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:27703206}. Cytoplasm {ECO:0000269|PubMed:27703206}.
CC Note=Shuttles between the nucleus and the cytoplasm. Actively
CC transported into the nucleus in an importin alpha/beta-dependent manner
CC (PubMed:27703206). Exported into the cytoplasm by CRM1
CC (PubMed:27703206). {ECO:0000269|PubMed:27703206}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:27703206}. Note=Imported into the nucleus when
CC incorporated in isoform 1/isoform 2 homodimer.
CC {ECO:0000269|PubMed:27703206}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1; Synonyms=TALDO1L {ECO:0000303|PubMed:27703206};
CC IsoId=Q93092-1; Sequence=Displayed;
CC Name=2; Synonyms=TALDO1S {ECO:0000303|PubMed:27703206};
CC IsoId=Q93092-2; Sequence=VSP_061596;
CC -!- DOMAIN: The first 10 amino acids are essential for nuclear
CC localization. {ECO:0000269|PubMed:27703206}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice develop normally; however, males
CC are sterile because of functional and structural defects of
CC mitochondria (PubMed:17003133). Mice spontaneously develop
CC hepatocellular carcinoma. The liver of these mice present an
CC accumulation of five-carbon sugarphosphates and a depletion of NADPH
CC and GSH (PubMed:19436114). {ECO:0000269|PubMed:17003133,
CC ECO:0000269|PubMed:19436114}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB08722.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U67611; AAB83955.1; -; mRNA.
DR EMBL; U63158; AAB08722.1; ALT_INIT; mRNA.
DR EMBL; U63159; AAB08723.1; -; mRNA.
DR EMBL; BC004754; AAH04754.1; -; mRNA.
DR EMBL; BC094277; AAH94277.1; -; mRNA.
DR CCDS; CCDS22011.1; -.
DR RefSeq; NP_035658.1; NM_011528.4.
DR PDB; 2CWN; X-ray; 2.10 A; A/B=13-337.
DR PDB; 2E1D; X-ray; 2.00 A; A/B=11-334.
DR PDBsum; 2CWN; -.
DR PDBsum; 2E1D; -.
DR AlphaFoldDB; Q93092; -.
DR SMR; Q93092; -.
DR BioGRID; 203964; 12.
DR IntAct; Q93092; 1.
DR STRING; 10090.ENSMUSP00000026576; -.
DR iPTMnet; Q93092; -.
DR PhosphoSitePlus; Q93092; -.
DR SwissPalm; Q93092; -.
DR REPRODUCTION-2DPAGE; IPI00124692; -.
DR REPRODUCTION-2DPAGE; Q93092; -.
DR CPTAC; non-CPTAC-3950; -.
DR EPD; Q93092; -.
DR jPOST; Q93092; -.
DR MaxQB; Q93092; -.
DR PaxDb; Q93092; -.
DR PeptideAtlas; Q93092; -.
DR PRIDE; Q93092; -.
DR ProteomicsDB; 263001; -.
DR Antibodypedia; 22640; 278 antibodies from 32 providers.
DR Ensembl; ENSMUST00000026576; ENSMUSP00000026576; ENSMUSG00000025503.
DR GeneID; 21351; -.
DR KEGG; mmu:21351; -.
DR UCSC; uc009kkv.2; mouse.
DR CTD; 6888; -.
DR MGI; MGI:1274789; Taldo1.
DR VEuPathDB; HostDB:ENSMUSG00000025503; -.
DR eggNOG; KOG2772; Eukaryota.
DR GeneTree; ENSGT00390000017361; -.
DR HOGENOM; CLU_047470_0_1_1; -.
DR InParanoid; Q93092; -.
DR OMA; KFGYKTL; -.
DR OrthoDB; 1402459at2759; -.
DR PhylomeDB; Q93092; -.
DR TreeFam; TF300757; -.
DR Reactome; R-MMU-163754; Insulin effects increased synthesis of Xylulose-5-Phosphate.
DR Reactome; R-MMU-71336; Pentose phosphate pathway.
DR UniPathway; UPA00115; UER00414.
DR BioGRID-ORCS; 21351; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Taldo1; mouse.
DR EvolutionaryTrace; Q93092; -.
DR PRO; PR:Q93092; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q93092; protein.
DR Bgee; ENSMUSG00000025503; Expressed in granulocyte and 265 other tissues.
DR ExpressionAtlas; Q93092; baseline and differential.
DR Genevisible; Q93092; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0048029; F:monosaccharide binding; ISO:MGI.
DR GO; GO:0004801; F:transaldolase activity; IDA:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISO:MGI.
DR GO; GO:0019682; P:glyceraldehyde-3-phosphate metabolic process; ISO:MGI.
DR GO; GO:0006098; P:pentose-phosphate shunt; IDA:MGI.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; ISO:MGI.
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 3D-structure; Acetylation; Alternative initiation; Cytoplasm;
KW Direct protein sequencing; Nucleus; Pentose shunt; Phosphoprotein;
KW Reference proteome; Schiff base; Transferase.
FT CHAIN 1..337
FT /note="Transaldolase"
FT /id="PRO_0000173565"
FT MOTIF 1..10
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:27703206"
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:0007744|PubMed:23806337"
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:21183079"
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:0007744|PubMed:23806337"
FT VAR_SEQ 1..10
FT /note="Missing (in isoform 2)"
FT /id="VSP_061596"
FT MUTAGEN 1
FT /note="M->A: Leads to expression of isoform 2 only."
FT /evidence="ECO:0000269|PubMed:27703206"
FT MUTAGEN 7
FT /note="K->A: Mainly expressed in the cytoplasm; when
FT associated with A-8 and A-10."
FT /evidence="ECO:0000269|PubMed:27703206"
FT MUTAGEN 8
FT /note="R->A: Mainly expressed in the cytoplasm; when
FT associated with A-7 and A-10."
FT /evidence="ECO:0000269|PubMed:27703206"
FT MUTAGEN 10
FT /note="R->A: Mainly expressed in the cytoplasm; when
FT associated with A-7 and A-8."
FT /evidence="ECO:0000269|PubMed:27703206"
FT MUTAGEN 11
FT /note="M->A: Leads to expression of isoform 1 only."
FT /evidence="ECO:0000269|PubMed:27703206"
FT CONFLICT 207..213
FT /note="EPQEDPG -> DPRKTW (in Ref. 1; AAB08723)"
FT /evidence="ECO:0000305"
FT HELIX 14..18
FT /evidence="ECO:0007829|PDB:2E1D"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:2E1D"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:2E1D"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:2E1D"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 59..72
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 76..98
FT /evidence="ECO:0007829|PDB:2E1D"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 115..131
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2E1D"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:2E1D"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:2E1D"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 212..226
FT /evidence="ECO:0007829|PDB:2E1D"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:2E1D"
FT TURN 246..249
FT /evidence="ECO:0007829|PDB:2E1D"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 257..265
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 291..299
FT /evidence="ECO:0007829|PDB:2E1D"
FT HELIX 302..330
FT /evidence="ECO:0007829|PDB:2E1D"
SQ SEQUENCE 337 AA; 37387 MW; B0AD351FD778367F CRC64;
MSGSPVKRQR MESALDQLKQ FTTVVADTGD FNAIDEYKPQ DATTNPSLIL AAAQMPAYQE
LVEEAIAYGK KLGGPQEEQI KNAIDKLFVL FGAEILKKIP GRVSTEVDAR LSFDKDAMVA
RARRLIELYK EAGVGKDRIL IKLSSTWEGI QAGKELEEQH GIHCNMTLLF SFAQAVACAE
AGVTLISPFV GRILDWHVAN TDKKSYEPQE DPGVKSVTKI YNYYKKFGYK TIVMGASFRN
TGEIKALAGC DFLTISPKLL GELLKDNSKL APALSVKAAQ TSDSEKIHLD EKAFRWLHNE
DQMAVEKLSD GIRKFAADAI KLERMLTERM FSAENGK
