ALDOA_MOUSE
ID ALDOA_MOUSE Reviewed; 364 AA.
AC P05064;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Fructose-bisphosphate aldolase A;
DE EC=4.1.2.13 {ECO:0000250|UniProtKB:P04075};
DE AltName: Full=Aldolase 1;
DE AltName: Full=Muscle-type aldolase;
GN Name=Aldoa; Synonyms=Aldo1;
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].
RC STRAIN=129;
RX PubMed=3697100; DOI=10.1093/nar/15.24.10595;
RA Mestek A., Stauffer J., Tolan D.R., Ciejek-Baez E.;
RT "Sequence of a mouse brain aldolase A cDNA.";
RL Nucleic Acids Res. 15:10595-10595(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-266 AND 295-364.
RX PubMed=2365699; DOI=10.1016/s0021-9258(19)38465-0;
RA Stauffer J.K., Colbert M.C., Ciejek-Baez E.;
RT "Nonconservative utilization of aldolase A alternative promoters.";
RL J. Biol. Chem. 265:11773-11782(1990).
RN [4]
RP PROTEIN SEQUENCE OF 2-22; 29-57; 61-109; 112-134; 154-258; 260-312 AND
RP 323-364, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 99-355.
RX PubMed=3009179; DOI=10.1111/j.1432-1033.1986.tb09572.x;
RA Paolella G., Buono P., Mancini P., Izzo P., Salvatore F.;
RT "Structure and expression of mouse aldolase genes. Brain-specific aldolase
RT C amino acid sequence is closely related to aldolase A.";
RL Eur. J. Biochem. 156:229-235(1986).
RN [6]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Catalyzes the reversible conversion of beta-D-fructose 1,6-
CC bisphosphate (FBP) into two triose phosphate and plays a key role in
CC glycolysis and gluconeogenesis (By similarity). In addition, may also
CC function as scaffolding protein (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P04075}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC Evidence={ECO:0000250|UniProtKB:P04075};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730;
CC Evidence={ECO:0000250|UniProtKB:P04075};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SUBUNIT: Homotetramer. Interacts with SNX9 and WAS. Interacts with
CC FBP2; the interaction blocks FBP2 inhibition by physiological
CC concentrations of AMP and reduces inhibition by Ca(2+) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band
CC {ECO:0000250|UniProtKB:P00883}. Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000250|UniProtKB:P00883}. Note=In skeletal muscle, accumulates
CC around the M line and within the I band, colocalizing with FBP2 on both
CC sides of the Z line in the absence of Ca(2+).
CC {ECO:0000250|UniProtKB:P00883}.
CC -!- MISCELLANEOUS: In vertebrates, three forms of this ubiquitous
CC glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver
CC and aldolase C in brain.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; X03797; CAA27423.1; -; mRNA.
DR EMBL; BC043026; AAH43026.1; -; mRNA.
DR EMBL; BC050896; AAH50896.1; -; mRNA.
DR EMBL; J05517; AAA37210.2; -; Genomic_DNA.
DR EMBL; Y00516; CAA68571.1; -; mRNA.
DR CCDS; CCDS21845.1; -.
DR PIR; S06323; ADMSA.
DR RefSeq; NP_001170779.1; NM_001177308.1.
DR RefSeq; NP_031464.1; NM_007438.4.
DR RefSeq; XP_006507273.1; XM_006507210.2.
DR RefSeq; XP_006507274.1; XM_006507211.3.
DR AlphaFoldDB; P05064; -.
DR SMR; P05064; -.
DR BioGRID; 198067; 31.
DR IntAct; P05064; 22.
DR MINT; P05064; -.
DR STRING; 10090.ENSMUSP00000084846; -.
DR MoonProt; P05064; -.
DR iPTMnet; P05064; -.
DR PhosphoSitePlus; P05064; -.
DR SwissPalm; P05064; -.
DR COMPLUYEAST-2DPAGE; P05064; -.
DR REPRODUCTION-2DPAGE; IPI00221402; -.
DR REPRODUCTION-2DPAGE; P05064; -.
DR SWISS-2DPAGE; P05064; -.
DR EPD; P05064; -.
DR jPOST; P05064; -.
DR PaxDb; P05064; -.
DR PeptideAtlas; P05064; -.
DR PRIDE; P05064; -.
DR ProteomicsDB; 296171; -.
DR TopDownProteomics; P05064; -.
DR DNASU; 11674; -.
DR Ensembl; ENSMUST00000032934; ENSMUSP00000032934; ENSMUSG00000030695.
DR Ensembl; ENSMUST00000106348; ENSMUSP00000101955; ENSMUSG00000030695.
DR GeneID; 11674; -.
DR KEGG; mmu:11674; -.
DR UCSC; uc009jsu.2; mouse.
DR CTD; 226; -.
DR MGI; MGI:87994; Aldoa.
DR VEuPathDB; HostDB:ENSMUSG00000030695; -.
DR eggNOG; KOG1557; Eukaryota.
DR GeneTree; ENSGT00950000182987; -.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; P05064; -.
DR OMA; DYREMLF; -.
DR PhylomeDB; P05064; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-70171; Glycolysis.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR SABIO-RK; P05064; -.
DR UniPathway; UPA00109; UER00183.
DR BioGRID-ORCS; 11674; 34 hits in 76 CRISPR screens.
DR ChiTaRS; Aldoa; mouse.
DR PRO; PR:P05064; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P05064; protein.
DR Bgee; ENSMUSG00000030695; Expressed in gastrocnemius medialis and 276 other tissues.
DR ExpressionAtlas; P05064; baseline and differential.
DR Genevisible; P05064; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0000792; C:heterochromatin; ISO:MGI.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0035686; C:sperm fibrous sheath; IDA:MGI.
DR GO; GO:0061827; C:sperm head; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0070061; F:fructose binding; ISO:MGI.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0006754; P:ATP biosynthetic process; ISO:MGI.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; ISO:MGI.
DR GO; GO:0061621; P:canonical glycolysis; IDA:MGI.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; ISO:MGI.
DR GO; GO:0006000; P:fructose metabolic process; ISO:MGI.
DR GO; GO:0006096; P:glycolytic process; ISS:UniProtKB.
DR GO; GO:0061615; P:glycolytic process through fructose-6-phosphate; IC:MGI.
DR GO; GO:0019242; P:methylglyoxal biosynthetic process; ISO:MGI.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:CAFA.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0006941; P:striated muscle contraction; ISO:MGI.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR029768; Aldolase_I_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Glycolysis;
KW Hydroxylation; Isopeptide bond; Lyase; Phosphoprotein; Reference proteome;
KW Schiff base; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..364
FT /note="Fructose-bisphosphate aldolase A"
FT /id="PRO_0000216937"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 230
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT BINDING 56
FT /ligand="substrate"
FT BINDING 147
FT /ligand="substrate"
FT SITE 364
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT MOD_RES 5
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P05065"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 42
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 99
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 111
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09972"
FT MOD_RES 111
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05065"
FT MOD_RES 147
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT MOD_RES 312
FT /note="N6-malonyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 330
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P04075"
FT CONFLICT 281
FT /note="S -> C (in Ref. 5; CAA27423)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 39356 MW; 0D067F7E4C63E216 CRC64;
MPHPYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR
QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN
GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC
TQKFSNEEIA MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF
SYGRALQASA LKAWGGKKEN LKAAQEEYIK RALANSLACQ GKYTPSGQSG AAASESLFIS
NHAY
