Fructose-bisphosphate aldolase C - Rattus norvegicus (Rat)

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P09117 (ALDOC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 108. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Fructose-bisphosphate aldolase C
EC=4.1.2.13

Alternative name(s):
Brain-type aldolase

Gene names

Name:

Aldoc

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	363 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Schiff base
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from direct assay PubMed 6405797. Source: RGD apoptotic process Inferred from mutant phenotype PubMed 16356555. Source: RGD fructose 1,6-bisphosphate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway organ regeneration Inferred from expression pattern PubMed 4430377. Source: RGD protein heterotetramerization Inferred from physical interaction PubMed 2188264. Source: RGD protein homotetramerization Inferred from direct assay PubMed 2188264. Source: RGD response to hypoxia Inferred from expression pattern PubMed 17053973. Source: RGD response to organic cyclic compound Inferred from expression pattern PubMed 18299792. Source: RGD response to organic nitrogen Inferred from expression pattern PubMed 18299792. Source: RGD
Cellular_component	axon Inferred from direct assay PubMed 19003905. Source: RGD cytoplasm Inferred from direct assay PubMed 201371. Source: RGD mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	fructose-bisphosphate aldolase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.5

Chain

2 – 363

362

Fructose-bisphosphate aldolase C

PRO_0000216951

Sites

Active site

188

Proton acceptor By similarity

Active site

230

Schiff-base intermediate with dihydroxyacetone-P

Binding site

Substrate

Binding site

147

Substrate

Site

363

Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

119

Phosphothreonine By similarity

Experimental info

Sequence conflict

337 – 339

LAA → ACS in CAA30044. Ref.2

Sequence conflict

337 – 339

LAA → ACS in CAA28889. Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

P09117 [UniParc].

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

363

39,284

        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' referencesShow '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, 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.
IPI	IPI00231736.
PIR	ADRTC. S00326.
RefSeq	NP_036629.1. NM_012497.1.
UniGene	Rn.11211.
3D structure databases
ProteinModelPortal	P09117.
SMR	P09117. Positions 3-344.
ModBase	Search...
Protein-protein interaction databases
IntAct	P09117. 1 interaction.
PTM databases
PhosphoSite	P09117.
2D gel databases
World-2DPAGE	0004:P09117.
Proteomic databases
PaxDb	P09117.
PRIDE	P09117.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000015535; ENSRNOP00000015535; ENSRNOG00000011452.
GeneID	24191.
KEGG	rno:24191.
Organism-specific databases
CTD	230.
RGD	2091. Aldoc.
Phylogenomic databases
eggNOG	COG3588.
GeneTree	ENSGT00390000010235.
HOGENOM	HOG000220876.
HOVERGEN	HBG002386.
InParanoid	P09117.
KO	K01623.
OrthoDB	EOG4X3H1J.
Enzyme and pathway databases
SABIO-RK	P09117.
UniPathway	UPA00109; UER00183.
Gene expression databases
ArrayExpress	P09117.
Genevestigator	P09117.
GermOnline	ENSRNOG00000011452. Rattus norvegicus.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR000741. Aldolase_I. IPR013785. Aldolase_TIM. [Graphical view]
PANTHER	PTHR11627. PTHR11627. 1 hit.
Pfam	PF00274. Glycolytic. 1 hit. [Graphical view]
PROSITE	PS00158. ALDOLASE_CLASS_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	602567.

Entry information

Entry name

ALDOC_RAT

Accession

Primary (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 3, 2013
This is version 108 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents