ALDOC_RAT
ID ALDOC_RAT Reviewed; 363 AA.
AC P09117; Q54AI4; Q63037;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Fructose-bisphosphate aldolase C;
DE EC=4.1.2.13;
DE AltName: Full=Brain-type aldolase;
GN Name=Aldoc;
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 [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=1993044; DOI=10.1016/0006-291x(91)91523-f;
RA Mukai T., Yatsuki H., Masuko S., Arai Y., Joh K., Hori K.;
RT "The structure of the brain-specific rat aldolase C gene and its regional
RT expression.";
RL Biochem. Biophys. Res. Commun. 174:1035-1042(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=2831050; DOI=10.1111/j.1432-1033.1988.tb13813.x;
RA Kukita A., Mukai T., Miyata T., Hori K.;
RT "The structure of brain-specific rat aldolase C mRNA and the evolution of
RT aldolase isozyme genes.";
RL Eur. J. Biochem. 171:471-478(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9443807; DOI=10.1093/oxfordjournals.jbchem.a021854;
RA Arai Y., Sugama T., Hashido K., Ohishi S., Mukai T.;
RT "The first exon of the rat aldolase C gene is essential for restoring the
RT chromatin structure in transgenic mice.";
RL J. Biochem. 122:927-938(1997).
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; 61-69; 73-96; 112-134; 158-215; 244-258;
RP 260-289; 305-315; 319-330 AND 343-363, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 251-363, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=3830170; DOI=10.1111/j.1432-1033.1987.tb10898.x;
RA Skala H., Vibert M., Lamas E., Maire P., Schweighoffer F., Kahn A.;
RT "Molecular cloning and expression of rat aldolase C messenger RNA during
RT development and hepatocarcinogenesis.";
RL Eur. J. Biochem. 163:513-518(1987).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-39, 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 -!- 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 -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SUBUNIT: Homotetramer. Interacts with ATP6V1E1 (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: High expression in the adult brain.
CC {ECO:0000269|PubMed:3830170}.
CC -!- DEVELOPMENTAL STAGE: Detected at low concentration in practically all
CC the fetal tissues and its expression markedly and rapidly decreased
CC after birth. {ECO:0000269|PubMed:3830170}.
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; M63656; AAA40717.1; -; Genomic_DNA.
DR EMBL; X06984; CAA30044.1; -; mRNA.
DR EMBL; AB017483; BAA75659.1; -; Genomic_DNA.
DR EMBL; BC099749; AAH99749.1; -; mRNA.
DR EMBL; X05277; CAA28889.1; -; mRNA.
DR PIR; S00326; ADRTC.
DR RefSeq; NP_036629.1; NM_012497.1.
DR AlphaFoldDB; P09117; -.
DR SMR; P09117; -.
DR BioGRID; 246381; 5.
DR IntAct; P09117; 2.
DR MINT; P09117; -.
DR STRING; 10116.ENSRNOP00000015535; -.
DR iPTMnet; P09117; -.
DR PhosphoSitePlus; P09117; -.
DR SwissPalm; P09117; -.
DR World-2DPAGE; 0004:P09117; -.
DR jPOST; P09117; -.
DR PaxDb; P09117; -.
DR PRIDE; P09117; -.
DR Ensembl; ENSRNOT00000015535; ENSRNOP00000015535; ENSRNOG00000011452.
DR GeneID; 24191; -.
DR KEGG; rno:24191; -.
DR CTD; 230; -.
DR RGD; 2091; Aldoc.
DR eggNOG; KOG1557; Eukaryota.
DR GeneTree; ENSGT00950000182987; -.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; P09117; -.
DR OrthoDB; 799973at2759; -.
DR PhylomeDB; P09117; -.
DR TreeFam; TF314203; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-70171; Glycolysis.
DR Reactome; R-RNO-70263; Gluconeogenesis.
DR SABIO-RK; P09117; -.
DR UniPathway; UPA00109; UER00183.
DR PRO; PR:P09117; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000011452; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; P09117; baseline and differential.
DR Genevisible; P09117; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0007568; P:aging; IDA:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0006915; P:apoptotic process; IMP:RGD.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; ISO:RGD.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP: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; Direct protein sequencing; Glycolysis; Lyase; Phosphoprotein;
KW Reference proteome; Schiff base.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5"
FT CHAIN 2..363
FT /note="Fructose-bisphosphate aldolase C"
FT /id="PRO_0000216951"
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 363
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 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09972"
FT MOD_RES 111
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09972"
FT CONFLICT 337..339
FT /note="LAA -> ACS (in Ref. 2; CAA30044 and 6; CAA28889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 39284 MW; 00FDB44B602FA9B3 CRC64;
MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR
QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQE KGILVGIKVD KGVVPLAGTD
GETTTQGLDG LLERCAQYKK DGADFAKWRC VLKISDRTPS ALAILENANV LARYASICQQ
NGIVPIVEPE ILPDGDHDLK RCQFVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC
PIKYSPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SLNLNAINRC SLPRPWALTF
SYGRALQASA LSAWRGQRDN AGAATEEFIK RAEMNGLAAQ GKYEGSGDGG AAAQSLYVAN
HAY
