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P05064 (ALDOA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 A

EC=4.1.2.13
Alternative name(s):
Aldolase 1
Muscle-type aldolase
Gene names
Name:Aldoa
Synonyms:Aldo1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein By similarity.

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 SNX9 and WAS. Interacts with FBP2; the interaction blocks FBP2 inhibition by physiological concentrations of AMP and reduces inhibition by Ca2+ By similarity.

Subcellular location

CytoplasmmyofibrilsarcomereI band. CytoplasmmyofibrilsarcomereM line. Note: In skeletal muscle, accumulates around the M line and within the I band, colocalizing with FBP2 on both sides of the Z line in the absence of Ca2+ By similarity.

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.4
Chain2 – 364363Fructose-bisphosphate aldolase A
PRO_0000216937

Sites

Active site1881Proton acceptor By similarity
Active site2301Schiff-base intermediate with dihydroxyacetone-P
Binding site561Substrate
Binding site1471Substrate
Site3641Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Amino acid modifications

Modified residue361Phosphoserine By similarity
Modified residue391Phosphoserine By similarity
Modified residue421N6-acetyllysine By similarity
Modified residue461Phosphoserine By similarity
Modified residue1081N6-acetyllysine By similarity
Modified residue1111N6-malonyllysine By similarity
Modified residue3121N6-malonyllysine By similarity
Modified residue3301N6-acetyllysine By similarity

Experimental info

Sequence conflict2811S → C in CAA27423. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P05064 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0D067F7E4C63E216

FASTA36439,356
        10         20         30         40         50         60 
MPHPYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR 

        70         80         90        100        110        120 
QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN 

       130        140        150        160        170        180 
GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ 

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

       250        260        270        280        290        300 
TQKFSNEEIA MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF 

       310        320        330        340        350        360 
SYGRALQASA LKAWGGKKEN LKAAQEEYIK RALANSLACQ GKYTPSGQSG AAASESLFIS 


NHAY 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of a mouse brain aldolase A cDNA."
Mestek A., Stauffer J., Tolan D.R., Ciejek-Baez E.
Nucleic Acids Res. 15:10595-10595(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129.
[2]"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].
Strain: C57BL/6.
Tissue: Brain.
[3]"Nonconservative utilization of aldolase A alternative promoters."
Stauffer J.K., Colbert M.C., Ciejek-Baez E.
J. Biol. Chem. 265:11773-11782(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-266 AND 295-364.
[4]Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-22; 29-57; 61-109; 112-134; 154-258; 260-312 AND 323-364, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[5]"Structure and expression of mouse aldolase genes. Brain-specific aldolase C amino acid sequence is closely related to aldolase A."
Paolella G., Buono P., Mancini P., Izzo P., Salvatore F.
Eur. J. Biochem. 156:229-235(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 99-355.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03797 mRNA. Translation: CAA27423.1.
BC043026 mRNA. Translation: AAH43026.1.
BC050896 mRNA. Translation: AAH50896.1.
J05517 Genomic DNA. Translation: AAA37210.2.
Y00516 mRNA. Translation: CAA68571.1.
CCDSCCDS21845.1.
PIRADMSA. S06323.
RefSeqNP_001170779.1. NM_001177308.1.
NP_031464.1. NM_007438.4.
XP_006507273.1. XM_006507210.1.
XP_006507274.1. XM_006507211.1.
UniGeneMm.275831.

3D structure databases

ProteinModelPortalP05064.
SMRP05064. Positions 5-344.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198067. 7 interactions.
IntActP05064. 20 interactions.
MINTMINT-1581489.

PTM databases

PhosphoSiteP05064.

2D gel databases

COMPLUYEAST-2DPAGEP05064.
REPRODUCTION-2DPAGEIPI00221402.
P05064.
SWISS-2DPAGEP05064.

Proteomic databases

MaxQBP05064.
PaxDbP05064.
PRIDEP05064.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032934; ENSMUSP00000032934; ENSMUSG00000030695.
ENSMUST00000106348; ENSMUSP00000101955; ENSMUSG00000030695.
GeneID11674.
KEGGmmu:11674.
UCSCuc009jsu.2. mouse.

Organism-specific databases

CTD226.
MGIMGI:87994. Aldoa.

Phylogenomic databases

eggNOGCOG3588.
HOGENOMHOG000220876.
HOVERGENHBG002386.
InParanoidP05064.
KOK01623.
OrthoDBEOG744T94.
PhylomeDBP05064.

Enzyme and pathway databases

SABIO-RKP05064.
UniPathwayUPA00109; UER00183.

Gene expression databases

ArrayExpressP05064.
BgeeP05064.
CleanExMM_ALDOA.
GenevestigatorP05064.

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

ChiTaRSALDOA. mouse.
NextBio279303.
PROP05064.
SOURCESearch...

Entry information

Entry nameALDOA_MOUSE
AccessionPrimary (citable) accession number: P05064
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 145 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot