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   24-JAN-2024, entry version 172.
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.ENSRNOP00000072735; -.
DR   GlyGen; P09117; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P09117; -.
DR   PhosphoSitePlus; P09117; -.
DR   SwissPalm; P09117; -.
DR   jPOST; P09117; -.
DR   PaxDb; 10116-ENSRNOP00000015535; -.
DR   Ensembl; ENSRNOT00000015535.9; ENSRNOP00000015535.4; ENSRNOG00000011452.9.
DR   Ensembl; ENSRNOT00055051392; ENSRNOP00055042358; ENSRNOG00055029644.
DR   Ensembl; ENSRNOT00060052103; ENSRNOP00060043333; ENSRNOG00060029953.
DR   Ensembl; ENSRNOT00065039729; ENSRNOP00065032317; ENSRNOG00065023213.
DR   GeneID; 24191; -.
DR   KEGG; rno:24191; -.
DR   AGR; RGD:2091; -.
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   OMA; GDAMQKW; -.
DR   OrthoDB; 3664741at2759; -.
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 cell types or tissues.
DR   ExpressionAtlas; P09117; baseline and differential.
DR   GO; GO:0030424; C:axon; 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:0031100; P:animal organ regeneration; IEP: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   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:SF3; FRUCTOSE-BISPHOSPHATE ALDOLASE C; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
DR   World-2DPAGE; 0004:P09117; -.
DR   Genevisible; P09117; RN.
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
//