Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P47738

- ALDH2_MOUSE

UniProt

P47738 - ALDH2_MOUSE

Protein

Aldehyde dehydrogenase, mitochondrial

Gene

Aldh2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Is capable of converting retinaldehyde to retinoic acid.

    Catalytic activityi

    An aldehyde + NAD+ + H2O = a carboxylate + NADH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei188 – 1881Transition state stabilizerBy similarity
    Active sitei287 – 2871Proton acceptorPROSITE-ProRule annotation
    Active sitei321 – 3211NucleophilePROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi264 – 2696NADBy similarity

    GO - Molecular functioni

    1. aldehyde dehydrogenase (NAD) activity Source: UniProtKB-EC
    2. protein binding Source: IntAct

    GO - Biological processi

    1. ethanol catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    UniPathwayiUPA00780; UER00768.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldehyde dehydrogenase, mitochondrial (EC:1.2.1.3)
    Alternative name(s):
    AHD-M1
    ALDH class 2
    ALDH-E2
    ALDHI
    Gene namesi
    Name:Aldh2
    Synonyms:Ahd-1, Ahd1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:99600. Aldh2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1919MitochondrionBy similarityAdd
    BLAST
    Chaini20 – 519500Aldehyde dehydrogenase, mitochondrialPRO_0000007169Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei20 – 201N-acetylserineCurated
    Modified residuei54 – 541N6-acetyllysine1 Publication
    Modified residuei75 – 751N6-acetyllysine1 Publication
    Modified residuei80 – 801N6-acetyllysine1 Publication
    Modified residuei161 – 1611N6-acetyllysine1 Publication
    Modified residuei370 – 3701N6-acetyllysine1 Publication
    Modified residuei377 – 3771N6-acetyllysine1 Publication
    Modified residuei385 – 3851N6-acetyllysine1 Publication
    Modified residuei409 – 4091N6-acetyllysine1 Publication
    Modified residuei428 – 4281N6-acetyllysine1 Publication
    Modified residuei430 – 4301N6-acetyllysine2 Publications
    Modified residuei443 – 4431N6-acetyllysine1 Publication
    Modified residuei453 – 4531N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP47738.
    PaxDbiP47738.
    PRIDEiP47738.

    2D gel databases

    REPRODUCTION-2DPAGEP47738.
    SWISS-2DPAGEP47738.
    UCD-2DPAGEP47738.

    PTM databases

    PhosphoSiteiP47738.

    Expressioni

    Inductioni

    By retinoic acid; 3-5 fold increase.

    Gene expression databases

    ArrayExpressiP47738.
    BgeeiP47738.
    CleanExiMM_ALDH2.
    GenevestigatoriP47738.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Sirt3Q8R1042EBI-2308120,EBI-6999888

    Protein-protein interaction databases

    IntActiP47738. 5 interactions.
    MINTiMINT-1859437.

    Structurei

    3D structure databases

    ProteinModelPortaliP47738.
    SMRiP47738. Positions 26-519.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1012.
    HOGENOMiHOG000271505.
    HOVERGENiHBG000097.
    InParanoidiP47738.
    KOiK00128.
    OMAiMACWKMA.
    OrthoDBiEOG7PS1F7.
    PhylomeDBiP47738.
    TreeFamiTF300455.

    Family and domain databases

    Gene3Di3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProiIPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR029510. Ald_DH_CS_GLU.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    [Graphical view]
    SUPFAMiSSF53720. SSF53720. 1 hit.
    PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P47738-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRAALTTVR RGPRLSRLLS AAATSAVPAP NHQPEVFCNQ IFINNEWHDA    50
    VSRKTFPTVN PSTGEVICQV AEGNKEDVDK AVKAARAAFQ LGSPWRRMDA 100
    SDRGRLLYRL ADLIERDRTY LAALETLDNG KPYVISYLVD LDMVLKCLRY 150
    YAGWADKYHG KTIPIDGDFF SYTRHEPVGV CGQIIPWNFP LLMQAWKLGP 200
    ALATGNVVVM KVAEQTPLTA LYVANLIKEA GFPPGVVNIV PGFGPTAGAA 250
    IASHEGVDKV AFTGSTEVGH LIQVAAGSSN LKRVTLELGG KSPNIIMSDA 300
    DMDWAVEQAH FALFFNQGQC CCAGSRTFVQ ENVYDEFVER SVARAKSRVV 350
    GNPFDSRTEQ GPQVDETQFK KILGYIKSGQ QEGAKLLCGG GAAADRGYFI 400
    QPTVFGDVKD GMTIAKEEIF GPVMQILKFK TIEEVVGRAN DSKYGLAAAV 450
    FTKDLDKANY LSQALQAGTV WINCYDVFGA QSPFGGYKMS GSGRELGEYG 500
    LQAYTEVKTV TVKVPQKNS 519
    Length:519
    Mass (Da):56,538
    Last modified:February 1, 1996 - v1
    Checksum:i200806F63D48F4DA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti88 – 892AF → C in AAC60691. (PubMed:8058062)Curated
    Sequence conflicti181 – 1811Missing in AAC60691. (PubMed:8058062)Curated
    Sequence conflicti227 – 2271I → S in AAC60691. (PubMed:8058062)Curated
    Sequence conflicti344 – 3441R → G in AAC60691. (PubMed:8058062)Curated
    Sequence conflicti370 – 3701K → N in AAC60691. (PubMed:8058062)Curated
    Sequence conflicti378 – 3781S → M in AAC60691. (PubMed:8058062)Curated
    Sequence conflicti476 – 4761D → V in AAC60691. (PubMed:8058062)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07235 mRNA. Translation: AAA64636.1.
    S71509 mRNA. Translation: AAC60691.1.
    BC005476 mRNA. Translation: AAH05476.1.
    Z32545 Genomic DNA. No translation available.
    CCDSiCCDS19638.1.
    PIRiI48966.
    RefSeqiNP_033786.1. NM_009656.3.
    UniGeneiMm.284446.

    Genome annotation databases

    EnsembliENSMUST00000031411; ENSMUSP00000031411; ENSMUSG00000029455.
    GeneIDi11669.
    KEGGimmu:11669.
    UCSCiuc008zjt.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07235 mRNA. Translation: AAA64636.1 .
    S71509 mRNA. Translation: AAC60691.1 .
    BC005476 mRNA. Translation: AAH05476.1 .
    Z32545 Genomic DNA. No translation available.
    CCDSi CCDS19638.1.
    PIRi I48966.
    RefSeqi NP_033786.1. NM_009656.3.
    UniGenei Mm.284446.

    3D structure databases

    ProteinModelPortali P47738.
    SMRi P47738. Positions 26-519.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P47738. 5 interactions.
    MINTi MINT-1859437.

    PTM databases

    PhosphoSitei P47738.

    2D gel databases

    REPRODUCTION-2DPAGE P47738.
    SWISS-2DPAGE P47738.
    UCD-2DPAGE P47738.

    Proteomic databases

    MaxQBi P47738.
    PaxDbi P47738.
    PRIDEi P47738.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031411 ; ENSMUSP00000031411 ; ENSMUSG00000029455 .
    GeneIDi 11669.
    KEGGi mmu:11669.
    UCSCi uc008zjt.1. mouse.

    Organism-specific databases

    CTDi 217.
    MGIi MGI:99600. Aldh2.

    Phylogenomic databases

    eggNOGi COG1012.
    HOGENOMi HOG000271505.
    HOVERGENi HBG000097.
    InParanoidi P47738.
    KOi K00128.
    OMAi MACWKMA.
    OrthoDBi EOG7PS1F7.
    PhylomeDBi P47738.
    TreeFami TF300455.

    Enzyme and pathway databases

    UniPathwayi UPA00780 ; UER00768 .

    Miscellaneous databases

    ChiTaRSi ALDH2. mouse.
    NextBioi 279291.
    PROi P47738.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P47738.
    Bgeei P47738.
    CleanExi MM_ALDH2.
    Genevestigatori P47738.

    Family and domain databases

    Gene3Di 3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProi IPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR029510. Ald_DH_CS_GLU.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    [Graphical view ]
    Pfami PF00171. Aldedh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53720. SSF53720. 1 hit.
    PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the gene encoding mouse mitochondrial aldehyde dehydrogenase."
      Chang C., Yoshida A.
      Gene 148:331-336(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6J.
    2. "Enzymatic conversion of retinaldehyde to retinoic acid by cloned murine cytosolic and mitochondrial aldehyde dehydrogenases."
      Chen M., Achkar C., Gudas L.J.
      Mol. Pharmacol. 46:88-96(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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].
      Strain: FVB/N.
      Tissue: Mammary gland.
    4. Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 54-80; 87-96; 162-174; 198-228; 260-282; 327-340; 349-370; 386-409; 417-428; 431-438 AND 444-453, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    5. "Isolation of genomic DNA fragments corresponding to genes modulated in vivo by a transcription factor."
      Caubin J., Iglesias T., Bernal J., Munoz A., Marquez G., Barbero J.L., Zaballos A.
      Nucleic Acids Res. 22:4132-4138(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 472-509.
    6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-430, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-75; LYS-80; LYS-161; LYS-370; LYS-377; LYS-385; LYS-409; LYS-428; LYS-430; LYS-443 AND LYS-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiALDH2_MOUSE
    AccessioniPrimary (citable) accession number: P47738
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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