ID   ALDOA_RAT               Reviewed;         364 AA.
AC   P05065; Q63038;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 189.
DE   RecName: Full=Fructose-bisphosphate aldolase A;
DE            EC=4.1.2.13 {ECO:0000250|UniProtKB:P04075};
DE   AltName: Full=Muscle-type aldolase;
GN   Name=Aldoa;
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].
RX   PubMed=3753977; DOI=10.1016/s0021-9258(17)35789-7;
RA   Mukai T., Joh K., Arai Y., Yatsuki H., Hori K.;
RT   "Tissue-specific expression of rat aldolase A mRNAs. Three molecular
RT   species differing only in the 5'-terminal sequences.";
RL   J. Biol. Chem. 261:3347-3354(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2416636; DOI=10.1016/0378-1119(85)90102-7;
RA   Joh K., Mukai T., Yatsuki H., Hori K.;
RT   "Rat aldolase A messenger RNA: the nucleotide sequence and multiple mRNA
RT   species with different 5'-terminal regions.";
RL   Gene 39:17-24(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3783705; DOI=10.1016/0022-2836(86)90011-2;
RA   Joh K., Arai Y., Mukai T., Hori K.;
RT   "Expression of three mRNA species from a single rat aldolase A gene,
RT   differing in their 5' non-coding regions.";
RL   J. Mol. Biol. 190:401-410(1986).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   [5]
RP   PROTEIN SEQUENCE OF 2-13; 15-22; 29-42; 70-99; 154-173; 209-215; 244-258;
RP   290-312 AND 332-364, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 324-356, AND TISSUE SPECIFICITY.
RC   STRAIN=Donryu; TISSUE=Hepatoma;
RX   PubMed=6086339; DOI=10.1111/j.1432-1033.1984.tb08264.x;
RA   Tsutsumi R., Tsutsumi K., Numazaki M., Ishikawa K.;
RT   "Two different aldolase A mRNA species in rat tissues.";
RL   Eur. J. Biochem. 142:161-164(1984).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-5; THR-9 AND SER-132, AND
RP   IDENTIFICATION BY 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 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   -!- INTERACTION:
CC       P05065; Q80Z30: Ppm1e; NbExp=2; IntAct=EBI-522118, EBI-7473061;
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   -!- TISSUE SPECIFICITY: Expressed in muscle, brain and hepatoma cells.
CC       {ECO:0000269|PubMed:6086339}.
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; M12919; AAA40714.1; -; mRNA.
DR   EMBL; M14420; AAA40715.1; -; mRNA.
DR   EMBL; X04261; CAA27815.1; -; Genomic_DNA.
DR   EMBL; X04262; CAA27815.1; JOINED; Genomic_DNA.
DR   EMBL; X04263; CAA27815.1; JOINED; Genomic_DNA.
DR   EMBL; X04264; CAA27815.1; JOINED; Genomic_DNA.
DR   EMBL; BC064440; AAH64440.1; -; mRNA.
DR   EMBL; M28282; AAA40720.1; -; mRNA.
DR   PIR; A24532; ADRTA.
DR   RefSeq; NP_001170776.1; NM_001177305.1.
DR   RefSeq; NP_001258465.1; NM_001271536.1.
DR   RefSeq; NP_036627.1; NM_012495.2.
DR   RefSeq; XP_006230273.1; XM_006230211.2.
DR   AlphaFoldDB; P05065; -.
DR   SMR; P05065; -.
DR   BioGRID; 246379; 6.
DR   IntAct; P05065; 8.
DR   MINT; P05065; -.
DR   STRING; 10116.ENSRNOP00000068764; -.
DR   GlyGen; P05065; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P05065; -.
DR   PhosphoSitePlus; P05065; -.
DR   jPOST; P05065; -.
DR   PaxDb; 10116-ENSRNOP00000032320; -.
DR   Ensembl; ENSRNOT00065028062; ENSRNOP00065022178; ENSRNOG00065016801.
DR   GeneID; 24189; -.
DR   KEGG; rno:24189; -.
DR   UCSC; RGD:2089; rat.
DR   AGR; RGD:2089; -.
DR   CTD; 226; -.
DR   RGD; 2089; Aldoa.
DR   VEuPathDB; HostDB:ENSRNOG00000052802; -.
DR   VEuPathDB; HostDB:ENSRNOG00000067655; -.
DR   eggNOG; KOG1557; Eukaryota.
DR   HOGENOM; CLU_031243_0_0_1; -.
DR   InParanoid; P05065; -.
DR   OrthoDB; 3664741at2759; -.
DR   PhylomeDB; P05065; -.
DR   Reactome; R-RNO-114608; Platelet degranulation.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   Reactome; R-RNO-70171; Glycolysis.
DR   Reactome; R-RNO-70263; Gluconeogenesis.
DR   SABIO-RK; P05065; -.
DR   UniPathway; UPA00109; UER00183.
DR   PRO; PR:P05065; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000052802; Expressed in skeletal muscle tissue and 20 other cell types or tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR   GO; GO:0000792; C:heterochromatin; IDA:WormBase.
DR   GO; GO:0031674; C:I band; IEA:UniProtKB-SubCell.
DR   GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR   GO; GO:0061827; C:sperm head; ISO:RGD.
DR   GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
DR   GO; GO:0070061; F:fructose binding; ISO:RGD.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0006754; P:ATP biosynthetic process; ISO:RGD.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; ISO:RGD.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; ISO:RGD.
DR   GO; GO:0006000; P:fructose metabolic process; ISO:RGD.
DR   GO; GO:0006096; P:glycolytic process; ISS:UniProtKB.
DR   GO; GO:0019242; P:methylglyoxal biosynthetic process; IMP:RGD.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; ISO:RGD.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR   GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR   GO; GO:0006941; P:striated muscle contraction; ISO:RGD.
DR   CDD; cd00948; FBP_aldolase_I_a; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR029768; Aldolase_I_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000741; FBA_I.
DR   NCBIfam; NF033379; FrucBisAld_I; 1.
DR   PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR11627:SF1; FRUCTOSE-BISPHOSPHATE ALDOLASE A; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
DR   World-2DPAGE; 0004:P05065; -.
DR   Genevisible; P05065; RN.
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:0000250|UniProtKB:P04075"
FT   CHAIN           2..364
FT                   /note="Fructose-bisphosphate aldolase A"
FT                   /id="PRO_0000216939"
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:0007744|PubMed:22673903"
FT   MOD_RES         9
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
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        145
FT                   /note="F -> S (in Ref. 2; AAA40715)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="M -> V (in Ref. 2; AAA40715)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        330
FT                   /note="K -> Q (in Ref. 6; AAA40720)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   364 AA;  39352 MW;  2774497C20DCC0DA CRC64;
     MPHPYPALTP EQKKELADIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR
     QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN
     GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS SLAIMENANV LARYASICQQ
     NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC
     TQKFSNEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF
     SYGRALQASA LKAWGGKKEN LKAAQEEYIK RALANSLACQ GKYTPSGQSG AAASESLFIS
     NHAY
//