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Protein

Fructose-bisphosphate aldolase C

Gene

Aldoc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Miscellaneous

In vertebrates, three forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain.

Catalytic activityi

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (Gpi)
  3. ATP-dependent 6-phosphofructokinase (Pfkm), ATP-dependent 6-phosphofructokinase, liver type (Pfkl), ATP-dependent 6-phosphofructokinase, platelet type (Pfkp), ATP-dependent 6-phosphofructokinase (Pfkm), ATP-dependent 6-phosphofructokinase (Pfkl), ATP-dependent 6-phosphofructokinase (Pfkp), ATP-dependent 6-phosphofructokinase, muscle type (Pfkm), ATP-dependent 6-phosphofructokinase (Pfkp)
  4. Fructose-bisphosphate aldolase (Aldoc), Fructose-bisphosphate aldolase (Aldoart2), Fructose-bisphosphate aldolase A (Aldoa), Fructose-bisphosphate aldolase B (Aldob), Fructose-bisphosphate aldolase C (Aldoc), Fructose-bisphosphate aldolase (Aldob)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei56Substrate1
Binding sitei147Substrate1
Active sitei188Proton acceptorBy similarity1
Active sitei230Schiff-base intermediate with dihydroxyacetone-P1
Sitei363Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate1

GO - Molecular functioni

  • fructose-bisphosphate aldolase activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • animal organ regeneration Source: RGD
  • apoptotic process Source: RGD
  • fructose 1,6-bisphosphate metabolic process Source: UniProtKB
  • glycolytic process Source: UniProtKB-UniPathway
  • protein heterotetramerization Source: RGD
  • protein homotetramerization Source: RGD
  • response to hypoxia Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to organonitrogen compound Source: RGD

Keywordsi

Molecular functionLyase
Biological processGlycolysis
LigandSchiff base

Enzyme and pathway databases

ReactomeiR-RNO-6798695 Neutrophil degranulation
R-RNO-70171 Glycolysis
R-RNO-70263 Gluconeogenesis
SABIO-RKiP09117
UniPathwayiUPA00109; UER00183

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase C (EC:4.1.2.13)
Alternative name(s):
Brain-type aldolase
Gene namesi
Name:Aldoc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi2091 Aldoc

Subcellular locationi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002169512 – 363Fructose-bisphosphate aldolase CAdd BLAST362

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5PhosphotyrosineBy similarity1
Modified residuei36PhosphoserineCombined sources1
Modified residuei39PhosphoserineCombined sources1
Modified residuei45PhosphoserineBy similarity1
Modified residuei111N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP09117
PRIDEiP09117

2D gel databases

World-2DPAGEi0004:P09117

PTM databases

iPTMnetiP09117
PhosphoSitePlusiP09117
SwissPalmiP09117

Expressioni

Tissue specificityi

High expression in the adult brain.1 Publication

Developmental stagei

Detected at low concentration in practically all the fetal tissues and its expression markedly and rapidly decreased after birth.1 Publication

Gene expression databases

BgeeiENSRNOG00000011452
ExpressionAtlasiP09117 baseline and differential
GenevisibleiP09117 RN

Interactioni

Subunit structurei

Homotetramer. Interacts with ATP6V1E1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi246381, 3 interactors
IntActiP09117, 1 interactor
STRINGi10116.ENSRNOP00000015535

Structurei

3D structure databases

ProteinModelPortaliP09117
SMRiP09117
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1557 Eukaryota
COG3588 LUCA
GeneTreeiENSGT00390000010235
HOGENOMiHOG000220876
HOVERGENiHBG002386
InParanoidiP09117
KOiK01623
PhylomeDBiP09117
TreeFamiTF314203

Family and domain databases

Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR029768 Aldolase_I_AS
IPR013785 Aldolase_TIM
IPR000741 FBA_I
PfamiView protein in Pfam
PF00274 Glycolytic, 1 hit
PROSITEiView protein in PROSITE
PS00158 ALDOLASE_CLASS_I, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09117-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE
60 70 80 90 100
NTEENRRLYR QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQE
110 120 130 140 150
KGILVGIKVD KGVVPLAGTD GETTTQGLDG LLERCAQYKK DGADFAKWRC
160 170 180 190 200
VLKISDRTPS ALAILENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK
210 220 230 240 250
RCQFVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC PIKYSPEEIA
260 270 280 290 300
MATVTALRRT VPPAVPGVTF LSGGQSEEEA SLNLNAINRC SLPRPWALTF
310 320 330 340 350
SYGRALQASA LSAWRGQRDN AGAATEEFIK RAEMNGLAAQ GKYEGSGDGG
360
AAAQSLYVAN HAY
Length:363
Mass (Da):39,284
Last modified:January 23, 2007 - v3
Checksum:i00FDB44B602FA9B3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti337 – 339LAA → ACS in CAA30044 (PubMed:2831050).Curated3
Sequence conflicti337 – 339LAA → ACS in CAA28889 (PubMed:3830170).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63656 Genomic DNA Translation: AAA40717.1
X06984 mRNA Translation: CAA30044.1
AB017483 Genomic DNA Translation: BAA75659.1
BC099749 mRNA Translation: AAH99749.1
X05277 mRNA Translation: CAA28889.1
PIRiS00326 ADRTC
RefSeqiNP_036629.1, NM_012497.1
UniGeneiRn.11211

Genome annotation databases

EnsembliENSRNOT00000015535; ENSRNOP00000015535; ENSRNOG00000011452
GeneIDi24191
KEGGirno:24191

Similar proteinsi

Entry informationi

Entry nameiALDOC_RAT
AccessioniPrimary (citable) accession number: P09117
Secondary accession number(s): Q54AI4, Q63037
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 144 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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