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P05063

- ALDOC_MOUSE

UniProt

P05063 - ALDOC_MOUSE

Protein

Fructose-bisphosphate aldolase C

Gene

Aldoc

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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
    Sitei363 – 3631Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

    GO - Molecular functioni

    1. fructose-bisphosphate aldolase activity Source: UniProtKB

    GO - Biological processi

    1. aging Source: Ensembl
    2. apoptotic process Source: Ensembl
    3. fructose 1,6-bisphosphate metabolic process Source: UniProtKB
    4. glycolytic process Source: UniProtKB-UniPathway
    5. organ regeneration Source: Ensembl
    6. protein heterotetramerization Source: Ensembl
    7. protein homotetramerization Source: Ensembl
    8. response to hypoxia Source: Ensembl
    9. response to organic cyclic compound Source: Ensembl
    10. response to organonitrogen compound Source: Ensembl

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Schiff base

    Enzyme and pathway databases

    SABIO-RKP05063.
    UniPathwayiUPA00109; UER00183.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-bisphosphate aldolase C (EC:4.1.2.13)
    Alternative name(s):
    Aldolase 3
    Brain-type aldolase
    Scrapie-responsive protein 2
    Zebrin II
    Gene namesi
    Name:Aldoc
    Synonyms:Aldo3, Scrg2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:101863. Aldoc.

    Subcellular locationi

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. mitochondrion Source: MGI

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 363362Fructose-bisphosphate aldolase CPRO_0000216949Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei111 – 1111N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP05063.
    PaxDbiP05063.
    PRIDEiP05063.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00119458.
    UCD-2DPAGEP05063.

    PTM databases

    PhosphoSiteiP05063.

    Expressioni

    Tissue specificityi

    Expressed exclusively in Purkinje cells in bands running from anterior to posterior across most of the cerebellum. Expressed at higher levels in the brains of BSE-infected animals.2 Publications

    Developmental stagei

    Expression begins in the first week of postnatal life.1 Publication

    Gene expression databases

    BgeeiP05063.
    CleanExiMM_ALDOC.
    GenevestigatoriP05063.

    Interactioni

    Subunit structurei

    Homotetramer. Interacts with ATP6V1E1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi198068. 1 interaction.
    IntActiP05063. 6 interactions.
    MINTiMINT-1864918.

    Structurei

    3D structure databases

    ProteinModelPortaliP05063.
    SMRiP05063. Positions 3-344.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG3588.
    GeneTreeiENSGT00390000010235.
    HOGENOMiHOG000220876.
    HOVERGENiHBG002386.
    InParanoidiP05063.
    KOiK01623.
    OMAiRGQQDNA.
    OrthoDBiEOG744T94.
    PhylomeDBiP05063.
    TreeFamiTF314203.

    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.

    P05063-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPHSYPALSA EQKKELSDIA LRIVTPGKGI LAADESVGSM AKRLSQIGVE    50
    NTEENRRLYR QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD 100
    KGILVGIKVD KGVVPLAGTD GETTTQGLDG LLERCAQYKK DGADFAKWRC 150
    VLKISDRTPS ALAILENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK 200
    RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC PIKYSPEEIA 250
    MATVTALRRT VPPAVPGVTF LSGGQSEEEA SLNLNAINRC PLPRPWALTF 300
    SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEMNGLAAQ GRYEGSGDGG 350
    AAAQSLYIAN HAY 363
    Length:363
    Mass (Da):39,395
    Last modified:January 23, 2007 - v4
    Checksum:i085C58AF163581C6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251T → A in AAH04802. (PubMed:15489334)Curated
    Sequence conflicti25 – 251T → A in AAH08184. (PubMed:15489334)Curated
    Sequence conflicti46 – 461Q → E in BAC30300. (PubMed:16141072)Curated
    Sequence conflicti62 – 621V → A in CAA27422. (PubMed:3009179)Curated
    Sequence conflicti113 – 1131V → L in CAA27422. (PubMed:3009179)Curated
    Sequence conflicti201 – 2011R → H in AAH04802. (PubMed:15489334)Curated
    Sequence conflicti201 – 2011R → H in AAH08184. (PubMed:15489334)Curated
    Sequence conflicti280 – 2801A → V in AAB32064. (PubMed:7925012)Curated
    Sequence conflicti358 – 3581I → V in AAH04802. (PubMed:15489334)Curated
    Sequence conflicti358 – 3581I → V in AAH08184. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S72537 mRNA. Translation: AAB32064.1.
    AK005077 mRNA. Translation: BAB23801.1.
    AK039267 mRNA. Translation: BAC30300.1.
    BC004802 mRNA. Translation: AAH04802.1.
    BC008184 mRNA. Translation: AAH08184.1.
    X03796 mRNA. Translation: CAA27422.1.
    AJ132391 mRNA. Translation: CAB77178.1.
    CCDSiCCDS25099.1.
    PIRiA25388. ADMSC.
    I53145.
    RefSeqiNP_033787.2. NM_009657.3.
    XP_006532096.1. XM_006532033.1.
    UniGeneiMm.7729.

    Genome annotation databases

    EnsembliENSMUST00000017534; ENSMUSP00000017534; ENSMUSG00000017390.
    ENSMUST00000102478; ENSMUSP00000099536; ENSMUSG00000017390.
    GeneIDi11676.
    KEGGimmu:11676.
    UCSCiuc007kiw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S72537 mRNA. Translation: AAB32064.1 .
    AK005077 mRNA. Translation: BAB23801.1 .
    AK039267 mRNA. Translation: BAC30300.1 .
    BC004802 mRNA. Translation: AAH04802.1 .
    BC008184 mRNA. Translation: AAH08184.1 .
    X03796 mRNA. Translation: CAA27422.1 .
    AJ132391 mRNA. Translation: CAB77178.1 .
    CCDSi CCDS25099.1.
    PIRi A25388. ADMSC.
    I53145.
    RefSeqi NP_033787.2. NM_009657.3.
    XP_006532096.1. XM_006532033.1.
    UniGenei Mm.7729.

    3D structure databases

    ProteinModelPortali P05063.
    SMRi P05063. Positions 3-344.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198068. 1 interaction.
    IntActi P05063. 6 interactions.
    MINTi MINT-1864918.

    PTM databases

    PhosphoSitei P05063.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00119458.
    UCD-2DPAGE P05063.

    Proteomic databases

    MaxQBi P05063.
    PaxDbi P05063.
    PRIDEi P05063.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000017534 ; ENSMUSP00000017534 ; ENSMUSG00000017390 .
    ENSMUST00000102478 ; ENSMUSP00000099536 ; ENSMUSG00000017390 .
    GeneIDi 11676.
    KEGGi mmu:11676.
    UCSCi uc007kiw.1. mouse.

    Organism-specific databases

    CTDi 230.
    MGIi MGI:101863. Aldoc.

    Phylogenomic databases

    eggNOGi COG3588.
    GeneTreei ENSGT00390000010235.
    HOGENOMi HOG000220876.
    HOVERGENi HBG002386.
    InParanoidi P05063.
    KOi K01623.
    OMAi RGQQDNA.
    OrthoDBi EOG744T94.
    PhylomeDBi P05063.
    TreeFami TF314203.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00183 .
    SABIO-RK P05063.

    Miscellaneous databases

    ChiTaRSi ALDOC. mouse.
    NextBioi 279307.
    PROi P05063.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05063.
    CleanExi MM_ALDOC.
    Genevestigatori P05063.

    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. "The cloning of zebrin II reveals its identity with aldolase C."
      Ahn A.H., Dziennis S., Hawkes R., Herrup K.
      Development 120:2081-2090(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: C57BL/6J.
      Tissue: Cerebellum.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Cerebellum and Spinal cord.
    3. "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: Mammary gland.
    4. "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 1-227.
    5. Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13; 29-57; 61-69; 73-96; 102-108; 112-134; 154-215; 244-258; 260-289; 305-315; 319-330 AND 332-363, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    6. "Enhanced levels of scrapie responsive gene mRNA in BSE-infected mouse brain."
      Dandoy-Dron F.C., Benboudjema L., Guillo F., Jaegly A., Jasmin C., Dormont D., Tovey M.G., Dron M.
      Brain Res. Mol. Brain Res. 76:173-179(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 281-363, TISSUE SPECIFICITY.
      Strain: BALB/c.
      Tissue: Brain.

    Entry informationi

    Entry nameiALDOC_MOUSE
    AccessioniPrimary (citable) accession number: P05063
    Secondary accession number(s): Q64011
    , Q8CA91, Q99K96, Q9DBA4, Q9JK32
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 147 of the entry and version 4 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3