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P05065

- ALDOA_RAT

UniProt

P05065 - ALDOA_RAT

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Protein

Fructose-bisphosphate aldolase A

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

Functioni

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

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 acceptor By similarity
Active sitei230 – 2301Schiff-base intermediate with dihydroxyacetone-P
Sitei364 – 3641Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

GO - Molecular functioni

  1. fructose-bisphosphate aldolase activity Source: UniProtKB
  2. protein binding Source: IntAct

GO - Biological processi

  1. glycolytic process Source: UniProtKB
  2. protein homotetramerization Source: UniProtKB
  3. response to estrogen Source: RGD
  4. response to heat Source: RGD
  5. response to hypoxia Source: RGD
  6. response to lipopolysaccharide Source: RGD
  7. response to nicotine 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-RKP05065.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase A (EC:4.1.2.13)
Alternative name(s):
Muscle-type aldolase
Gene namesi
Name:Aldoa
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi2089. Aldoa.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. M band Source: UniProtKB-SubCell
  3. membrane Source: Ensembl
  4. mitochondrion Source: RGD
  5. protein complex Source: Ensembl
  6. Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 364363Fructose-bisphosphate aldolase APRO_0000216939Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361Phosphoserine By similarity
Modified residuei39 – 391Phosphoserine By similarity
Modified residuei42 – 421N6-acetyllysine By similarity
Modified residuei46 – 461Phosphoserine By similarity
Modified residuei108 – 1081N6-acetyllysine By similarity
Modified residuei111 – 1111N6-malonyllysine By similarity
Modified residuei312 – 3121N6-malonyllysine By similarity
Modified residuei330 – 3301N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP05065.
PRIDEiP05065.

2D gel databases

World-2DPAGE0004:P05065.

PTM databases

PhosphoSiteiP05065.

Expressioni

Tissue specificityi

Expressed in muscle, brain and hepatoma cells.1 Publication

Gene expression databases

ArrayExpressiP05065.
GenevestigatoriP05065.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
Ppm1eQ80Z302EBI-522118,EBI-7473061

Protein-protein interaction databases

BioGridi246379. 3 interactions.
IntActiP05065. 6 interactions.
MINTiMINT-4567674.
STRINGi10116.ENSRNOP00000031940.

Structurei

3D structure databases

ProteinModelPortaliP05065.
SMRiP05065. Positions 5-344.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3588.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP05065.
KOiK01623.
OMAiWRAVIAI.
OrthoDBiEOG744T94.
PhylomeDBiP05065.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view]
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.

P05065-1 [UniParc]FASTAAdd to Basket

« Hide

MPHPYPALTP EQKKELADIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE    50
NTEENRRFYR QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS 100
KGGVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRC 150
VLKIGEHTPS SLAIMENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK 200
RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC TQKFSNEEIA 250
MATVTALRRT VPPAVPGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF 300
SYGRALQASA LKAWGGKKEN LKAAQEEYIK RALANSLACQ GKYTPSGQSG 350
AAASESLFIS NHAY 364
Length:364
Mass (Da):39,352
Last modified:January 23, 2007 - v2
Checksum:i2774497C20DCC0DA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451F → S in AAA40715. 1 Publication
Sequence conflicti165 – 1651M → V in AAA40715. 1 Publication
Sequence conflicti330 – 3301K → Q in AAA40720. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12919 mRNA. Translation: AAA40714.1.
M14420 mRNA. Translation: AAA40715.1.
X04261
, X04262, X04263, X04264 Genomic DNA. Translation: CAA27815.1.
BC064440 mRNA. Translation: AAH64440.1.
M28282 mRNA. Translation: AAA40720.1.
PIRiA24532. ADRTA.
RefSeqiNP_001170776.1. NM_001177305.1.
NP_001258465.1. NM_001271536.1.
NP_036627.1. NM_012495.2.
XP_006230273.1. XM_006230211.1.
UniGeneiRn.1774.

Genome annotation databases

EnsembliENSRNOT00000032362; ENSRNOP00000032320; ENSRNOG00000023647.
GeneIDi24189.
KEGGirno:24189.
UCSCiRGD:2089. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12919 mRNA. Translation: AAA40714.1 .
M14420 mRNA. Translation: AAA40715.1 .
X04261
, X04262 , X04263 , X04264 Genomic DNA. Translation: CAA27815.1 .
BC064440 mRNA. Translation: AAH64440.1 .
M28282 mRNA. Translation: AAA40720.1 .
PIRi A24532. ADRTA.
RefSeqi NP_001170776.1. NM_001177305.1.
NP_001258465.1. NM_001271536.1.
NP_036627.1. NM_012495.2.
XP_006230273.1. XM_006230211.1.
UniGenei Rn.1774.

3D structure databases

ProteinModelPortali P05065.
SMRi P05065. Positions 5-344.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 246379. 3 interactions.
IntActi P05065. 6 interactions.
MINTi MINT-4567674.
STRINGi 10116.ENSRNOP00000031940.

PTM databases

PhosphoSitei P05065.

2D gel databases

World-2DPAGE 0004:P05065.

Proteomic databases

PaxDbi P05065.
PRIDEi P05065.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000032362 ; ENSRNOP00000032320 ; ENSRNOG00000023647 .
GeneIDi 24189.
KEGGi rno:24189.
UCSCi RGD:2089. rat.

Organism-specific databases

CTDi 226.
RGDi 2089. Aldoa.

Phylogenomic databases

eggNOGi COG3588.
GeneTreei ENSGT00390000010235.
HOGENOMi HOG000220876.
HOVERGENi HBG002386.
InParanoidi P05065.
KOi K01623.
OMAi WRAVIAI.
OrthoDBi EOG744T94.
PhylomeDBi P05065.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00183 .
Reactomei REACT_217998. Gluconeogenesis.
REACT_225694. Glycolysis.
SABIO-RK P05065.

Miscellaneous databases

NextBioi 602559.
PROi P05065.

Gene expression databases

ArrayExpressi P05065.
Genevestigatori P05065.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view ]
Pfami PF00274. Glycolytic. 1 hit.
[Graphical view ]
PROSITEi PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Tissue-specific expression of rat aldolase A mRNAs. Three molecular species differing only in the 5'-terminal sequences."
    Mukai T., Joh K., Arai Y., Yatsuki H., Hori K.
    J. Biol. Chem. 261:3347-3354(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Rat aldolase A messenger RNA: the nucleotide sequence and multiple mRNA species with different 5'-terminal regions."
    Joh K., Mukai T., Yatsuki H., Hori K.
    Gene 39:17-24(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Expression of three mRNA species from a single rat aldolase A gene, differing in their 5' non-coding regions."
    Joh K., Arai Y., Mukai T., Hori K.
    J. Mol. Biol. 190:401-410(1986) [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., Chen W.-Q., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 15-22; 29-42; 70-99; 154-173; 209-215; 244-258; 290-312 AND 332-364, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Spinal cord.
  6. "Two different aldolase A mRNA species in rat tissues."
    Tsutsumi R., Tsutsumi K., Numazaki M., Ishikawa K.
    Eur. J. Biochem. 142:161-164(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 324-356, TISSUE SPECIFICITY.
    Strain: Donryu.
    Tissue: Hepatoma.

Entry informationi

Entry nameiALDOA_RAT
AccessioniPrimary (citable) accession number: P05065
Secondary accession number(s): Q63038
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 132 of the entry and version 2 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

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