ALDOA_RAT
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 03-AUG-2022, entry version 183.
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.ENSRNOP00000032320; -.
DR iPTMnet; P05065; -.
DR PhosphoSitePlus; P05065; -.
DR World-2DPAGE; 0004:P05065; -.
DR jPOST; P05065; -.
DR PaxDb; P05065; -.
DR PRIDE; P05065; -.
DR GeneID; 24189; -.
DR KEGG; rno:24189; -.
DR UCSC; RGD:2089; rat.
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 OMA; DYREMLF; -.
DR OrthoDB; 799973at2759; -.
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 tissues.
DR Genevisible; P05065; RN.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0000792; C:heterochromatin; IDA:WormBase.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0035686; C:sperm fibrous sheath; ISO:RGD.
DR GO; GO:0061827; C:sperm head; ISO:RGD.
DR GO; GO:0030018; C:Z disc; 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:0002020; F:protease 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:0061621; P:canonical glycolysis; 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:0030335; P:positive regulation of cell migration; 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:0009408; P:response to heat; 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 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: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
