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Protein

Fructose-bisphosphate aldolase C

Gene

Aldoc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561Substrate
Binding sitei147 – 1471Substrate
Active sitei188 – 1881Proton acceptorBy similarity
Active sitei230 – 2301Schiff-base intermediate with dihydroxyacetone-P
Sitei363 – 3631Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

GO - Molecular functioni

  1. fructose-bisphosphate aldolase activity Source: UniProtKB

GO - Biological processi

  1. aging Source: RGD
  2. apoptotic process Source: RGD
  3. epithelial cell differentiation Source: Ensembl
  4. fructose 1,6-bisphosphate metabolic process Source: UniProtKB
  5. glycolytic process Source: UniProtKB-UniPathway
  6. organ regeneration Source: RGD
  7. protein heterotetramerization Source: RGD
  8. protein homotetramerization Source: RGD
  9. response to hypoxia Source: RGD
  10. response to organic cyclic compound Source: RGD
  11. response to organonitrogen compound Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

ReactomeiREACT_217998. Gluconeogenesis.
REACT_225694. Glycolysis.
SABIO-RKP09117.
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi2091. Aldoc.

Subcellular locationi

GO - Cellular componenti

  1. axon Source: RGD
  2. cytoplasm Source: RGD
  3. extracellular vesicular exosome Source: Ensembl
  4. mitochondrion Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 363362Fructose-bisphosphate aldolase CPRO_0000216951Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP09117.
PRIDEiP09117.

2D gel databases

World-2DPAGE0004:P09117.

PTM databases

PhosphoSiteiP09117.

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

ExpressionAtlasiP09117. baseline and differential.
GenevestigatoriP09117.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi246381. 3 interactions.
IntActiP09117. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP09117.
SMRiP09117. Positions 3-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3588.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP09117.
KOiK01623.
OMAiWRGQQDN.
OrthoDBiEOG744T94.
PhylomeDBiP09117.
TreeFamiTF314203.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view]
PANTHERiPTHR11627. PTHR11627. 1 hit.
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti337 – 3393LAA → ACS in CAA30044. (PubMed:2831050)Curated
Sequence conflicti337 – 3393LAA → ACS in CAA28889. (PubMed:3830170)Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP09117.
SMRiP09117. Positions 3-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246381. 3 interactions.
IntActiP09117. 1 interaction.

PTM databases

PhosphoSiteiP09117.

2D gel databases

World-2DPAGE0004:P09117.

Proteomic databases

PaxDbiP09117.
PRIDEiP09117.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000015535; ENSRNOP00000015535; ENSRNOG00000011452.
GeneIDi24191.
KEGGirno:24191.

Organism-specific databases

CTDi230.
RGDi2091. Aldoc.

Phylogenomic databases

eggNOGiCOG3588.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP09117.
KOiK01623.
OMAiWRGQQDN.
OrthoDBiEOG744T94.
PhylomeDBiP09117.
TreeFamiTF314203.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
ReactomeiREACT_217998. Gluconeogenesis.
REACT_225694. Glycolysis.
SABIO-RKP09117.

Miscellaneous databases

NextBioi602567.

Gene expression databases

ExpressionAtlasiP09117. baseline and differential.
GenevestigatoriP09117.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view]
PANTHERiPTHR11627. PTHR11627. 1 hit.
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The structure of the brain-specific rat aldolase C gene and its regional expression."
    Mukai T., Yatsuki H., Masuko S., Arai Y., Joh K., Hori K.
    Biochem. Biophys. Res. Commun. 174:1035-1042(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Brain.
  2. "The structure of brain-specific rat aldolase C mRNA and the evolution of aldolase isozyme genes."
    Kukita A., Mukai T., Miyata T., Hori K.
    Eur. J. Biochem. 171:471-478(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "The first exon of the rat aldolase C gene is essential for restoring the chromatin structure in transgenic mice."
    Arai Y., Sugama T., Hashido K., Ohishi S., Mukai T.
    J. Biochem. 122:927-938(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  5. Lubec G., Afjehi-Sadat L., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 15-22; 61-69; 73-96; 112-134; 158-215; 244-258; 260-289; 305-315; 319-330 AND 343-363, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Spinal cord.
  6. "Molecular cloning and expression of rat aldolase C messenger RNA during development and hepatocarcinogenesis."
    Skala H., Vibert M., Lamas E., Maire P., Schweighoffer F., Kahn A.
    Eur. J. Biochem. 163:513-518(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 251-363, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Wistar.
    Tissue: Brain.

Entry informationi

Entry nameiALDOC_RAT
AccessioniPrimary (citable) accession number: P09117
Secondary accession number(s): Q54AI4, Q63037
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.