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P05065

- ALDOA_RAT

UniProt

P05065 - ALDOA_RAT

Protein

Fructose-bisphosphate aldolase A

Gene

Aldoa

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

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

    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

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei36 – 361PhosphoserineBy similarity
    Modified residuei39 – 391PhosphoserineBy similarity
    Modified residuei42 – 421N6-acetyllysineBy similarity
    Modified residuei46 – 461PhosphoserineBy similarity
    Modified residuei108 – 1081N6-acetyllysineBy similarity
    Modified residuei111 – 1111N6-malonyllysineBy similarity
    Modified residuei312 – 3121N6-malonyllysineBy similarity
    Modified residuei330 – 3301N6-acetyllysineBy 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.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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti145 – 1451F → S in AAA40715. (PubMed:2416636)Curated
    Sequence conflicti165 – 1651M → V in AAA40715. (PubMed:2416636)Curated
    Sequence conflicti330 – 3301K → Q in AAA40720. (PubMed:6086339)Curated

    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

    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: October 1, 2014
    This is version 133 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