[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3753977 [NCBI, ExPASy, EBI, Israel, Japan] Mukai T., Joh K., Arai Y., Yatsuki H., Hori K.; "Tissue-specific expression of rat aldolase A mRNAs. Three molecular species differing only in the 5'-terminal sequences."; J. Biol. Chem. 261:3347-3354(1986).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0378-1119(85)90102-7; PubMed=2416636 [NCBI, ExPASy, EBI, Israel, Japan] Joh K., Mukai T., Yatsuki H., Hori K.; "Rat aldolase A messenger RNA: the nucleotide sequence and multiple mRNA species with different 5'-terminal regions."; Gene 39:17-24(1985).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0022-2836(86)90011-2; PubMed=3783705 [NCBI, ExPASy, EBI, Israel, Japan] Joh K., Arai Y., Mukai T., Hori K.; "Expression of three mRNA species from a single rat aldolase A gene, differing in their 5' non-coding regions."; J. Mol. Biol. 190:401-410(1986).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Prostate; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	PROTEIN SEQUENCE OF 2-13; 15-22; 29-42; 70-99; 154-173; 209-215; 244-258; 290-312 AND 332-364, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord; Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.; Submitted (JUL-2007) to UniProtKB.
[6]	NUCLEOTIDE SEQUENCE [MRNA] OF 324-356, AND TISSUE SPECIFICITY. STRAIN=Donryu; TISSUE=Hepatoma; DOI=10.1111/j.1432-1033.1984.tb08264.x; PubMed=6086339 [NCBI, ExPASy, EBI, Israel, Japan] Tsutsumi R., Tsutsumi K., Numazaki M., Ishikawa K.; "Two different aldolase A mRNA species in rat tissues."; Eur. J. Biochem. 142:161-164(1984).

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: Homotetramer.
TISSUE SPECIFICITY: Expressed in muscle, brain and hepatoma cells.
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.
SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M12919; AAA40714.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M14420; AAA40715.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04261; CAA27815.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04262; CAA27815.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04263; CAA27815.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04264; CAA27815.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC064440; AAH64440.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M28282; AAA40720.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A24532; ADRTA.

NP_036627.1; -.

3D structure databases

HSSP

P00883; 1ADO. [HSSP ENTRY / PDB]

P05065; 2-364.

PTM databases

P05065; -.

2D gel databases

Rat-heart-2DPAGE

P05065; -.

Organism-specific databases

RGD

2089; Aldoa.

Gene expression databases

ArrayExpress

P05065; -.

GermOnline

ENSRNOG00000023647; Rattus norvegicus.

Family and domain databases

InterPro

IPR000741; Aldolase_I.
IPR013785; Aldolase_TIM.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

PANTHER

PTHR11627; Aldolase_I; 1.

Pfam

PF00274; Glycolytic; 1.
Pfam graphical view of domain structure.

ProDom

PD001128; Aldolase_I; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00158; ALDOLASE_CLASS_I; 1.

Genome annotation databases

Ensembl

ENSRNOG00000023647; Rattus norvegicus. [Contig view]

GeneID

24189; -.

KEGG

rno:24189; -.

Phylogenomic databases

HOVERGEN

P05065; -.

Other

NextBio

602559; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Direct protein sequencing; Glycolysis; Lyase; Phosphoprotein; Schiff base.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 364`	`363`	`Fructose-bisphosphate aldolase A.`	`PRO_0000216939`
`ACT_SITE`	`188 188`		`Proton acceptor (By similarity).`
`ACT_SITE`	`230 230`		`Schiff-base intermediate with dihydroxyacetone-P.`
`BINDING`	`56 56`		`Substrate.`
`BINDING`	`147 147`		`Substrate.`
`SITE`	`364 364`	`1`	`Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate.`
`MOD_RES`	`5 5`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`13 13`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`36 36`		`Phosphoserine (By similarity).`
`MOD_RES`	`39 39`		`Phosphoserine (By similarity).`
`MOD_RES`	`42 42`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`46 46`		`Phosphoserine (By similarity).`
`MOD_RES`	`65 65`		`Phosphothreonine (By similarity).`
`MOD_RES`	`204 204`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`223 223`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`235 235`		`Phosphothreonine (By similarity).`
`MOD_RES`	`241 241`		`Phosphothreonine (By similarity).`
`MOD_RES`	`354 354`		`Phosphoserine (By similarity).`
`MOD_RES`	`356 356`		`Phosphoserine (By similarity).`
`CONFLICT`	`145 145`		`F -> S (in Ref. 2; AAA40715).`
`CONFLICT`	`165 165`		`M -> V (in Ref. 2; AAA40715).`
`CONFLICT`	`330 330`		`K -> Q (in Ref. 6; AAA40720).`

Sequence information

Length: 364 AA [This is the length of the unprocessed precursor]

Molecular weight: 39352 Da [This is the MW of the unprocessed precursor]

CRC64: 2774497C20DCC0DA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPHPYPALTP EQKKELADIA 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 SLAIMENANV LARYASICQQ 

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

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

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


NHAY

P05065 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools