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P47738

- ALDH2_MOUSE

UniProt

P47738 - ALDH2_MOUSE

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Protein
Aldehyde dehydrogenase, mitochondrial
Gene
Aldh2, Ahd-1, Ahd1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 stabilizer By similarity
Active sitei287 – 2871Proton acceptor By similarity
Active sitei321 – 3211Nucleophile By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi264 – 2696NAD By 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1919Mitochondrion By similarity
Add
BLAST
Chaini20 – 519500Aldehyde dehydrogenase, mitochondrial
PRO_0000007169Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201N-acetylserine Inferred
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.

Family & Domainsi

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 892AF → C in AAC60691. 1 Publication
Sequence conflicti181 – 1811Missing in AAC60691. 1 Publication
Sequence conflicti227 – 2271I → S in AAC60691. 1 Publication
Sequence conflicti344 – 3441R → G in AAC60691. 1 Publication
Sequence conflicti370 – 3701K → N in AAC60691. 1 Publication
Sequence conflicti378 – 3781S → M in AAC60691. 1 Publication
Sequence conflicti476 – 4761D → V in AAC60691. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 124 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

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