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P09117 (ALDOC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase C

EC=4.1.2.13
Alternative name(s):
Brain-type aldolase
Gene names
Name:Aldoc
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

Subunit structure

Homotetramer. Interacts with ATP6V1E1 By similarity.

Tissue specificity

High expression in the adult brain. Ref.6

Developmental stage

Detected at low concentration in practically all the fetal tissues and its expression markedly and rapidly decreased after birth. Ref.6

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.

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 363362Fructose-bisphosphate aldolase C
PRO_0000216951

Sites

Active site1881Proton acceptor By similarity
Active site2301Schiff-base intermediate with dihydroxyacetone-P
Binding site561Substrate
Binding site1471Substrate
Site3631Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Amino acid modifications

Modified residue1111N6-acetyllysine By similarity

Experimental info

Sequence conflict337 – 3393LAA → ACS in CAA30044. Ref.2
Sequence conflict337 – 3393LAA → ACS in CAA28889. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P09117 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 00FDB44B602FA9B3

FASTA36339,284
        10         20         30         40         50         60 
MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR 

        70         80         90        100        110        120 
QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQE KGILVGIKVD KGVVPLAGTD 

       130        140        150        160        170        180 
GETTTQGLDG LLERCAQYKK DGADFAKWRC VLKISDRTPS ALAILENANV LARYASICQQ 

       190        200        210        220        230        240 
NGIVPIVEPE ILPDGDHDLK RCQFVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC 

       250        260        270        280        290        300 
PIKYSPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SLNLNAINRC SLPRPWALTF 

       310        320        330        340        350        360 
SYGRALQASA LSAWRGQRDN AGAATEEFIK RAEMNGLAAQ GKYEGSGDGG AAAQSLYVAN 


HAY 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRADRTC. S00326.
RefSeqNP_036629.1. NM_012497.1.
UniGeneRn.11211.

3D structure databases

ProteinModelPortalP09117.
SMRP09117. Positions 3-344.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246381. 3 interactions.
IntActP09117. 1 interaction.

PTM databases

PhosphoSiteP09117.

2D gel databases

World-2DPAGE0004:P09117.

Proteomic databases

PaxDbP09117.
PRIDEP09117.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000015535; ENSRNOP00000015535; ENSRNOG00000011452.
GeneID24191.
KEGGrno:24191.

Organism-specific databases

CTD230.
RGD2091. Aldoc.

Phylogenomic databases

eggNOGCOG3588.
GeneTreeENSGT00390000010235.
HOGENOMHOG000220876.
HOVERGENHBG002386.
InParanoidP09117.
KOK01623.
OMARGQQDNA.
OrthoDBEOG744T94.
PhylomeDBP09117.
TreeFamTF314203.

Enzyme and pathway databases

SABIO-RKP09117.
UniPathwayUPA00109; UER00183.

Gene expression databases

ArrayExpressP09117.
GenevestigatorP09117.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERPTHR11627. PTHR11627. 1 hit.
PfamPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio602567.

Entry information

Entry nameALDOC_RAT
AccessionPrimary (citable) accession number: P09117
Secondary accession number(s): Q54AI4, Q63037
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways