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P11884

- ALDH2_RAT

UniProt

P11884 - ALDH2_RAT

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Protein
Aldehyde dehydrogenase, mitochondrial
Gene
Aldh2
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei188 – 1881Transition state stabilizer
Active sitei287 – 2871Proton acceptor
Active sitei321 – 3211Nucleophile

Regions

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

GO - Molecular functioni

  1. NADH binding Source: RGD
  2. aldehyde dehydrogenase (NAD) activity Source: RGD
  3. identical protein binding Source: RGD
Complete GO annotation...

GO - Biological processi

  1. cellular response to fatty acid Source: RGD
  2. cellular response to hormone stimulus Source: RGD
  3. ethanol catabolic process Source: UniProtKB-UniPathway
  4. liver development Source: RGD
  5. negative regulation of apoptotic process Source: RGD
  6. response to estradiol Source: RGD
  7. response to hyperoxia Source: RGD
  8. response to lipopolysaccharide Source: RGD
  9. response to nicotine Source: RGD
  10. response to progesterone Source: RGD
  11. response to testosterone Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

SABIO-RKP11884.
UniPathwayiUPA00780; UER00768.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde dehydrogenase, mitochondrial (EC:1.2.1.3)
Alternative name(s):
ALDH class 2
ALDH-E2
ALDH1
Gene namesi
Name:Aldh2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi69219. Aldh2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1919Mitochondrion
Add
BLAST
Chaini20 – 519500Aldehyde dehydrogenase, mitochondrial
PRO_0000007170Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201N-acetylserine Inferred
Modified residuei54 – 541N6-acetyllysine By similarity
Modified residuei75 – 751N6-acetyllysine By similarity
Modified residuei80 – 801N6-acetyllysine By similarity
Modified residuei161 – 1611N6-acetyllysine By similarity
Modified residuei370 – 3701N6-acetyllysine By similarity
Modified residuei377 – 3771N6-acetyllysine By similarity
Modified residuei385 – 3851N6-acetyllysine By similarity
Modified residuei409 – 4091N6-acetyllysine By similarity
Modified residuei428 – 4281N6-acetyllysine By similarity
Modified residuei430 – 4301N6-acetyllysine By similarity
Modified residuei443 – 4431N6-acetyllysine By similarity
Modified residuei453 – 4531N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP11884.
PRIDEiP11884.

2D gel databases

World-2DPAGE0004:P11884.

PTM databases

PhosphoSiteiP11884.

Expressioni

Gene expression databases

GenevestigatoriP11884.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiP11884. 2 interactions.
MINTiMINT-4569918.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 206

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OM2NMR-B12-20[»]
2V1SX-ray2.05H/I/J/K/L/M/N12-24[»]
2V1TX-ray1.92C/D12-22[»]
3AWRX-ray2.00C/D12-20[»]
3AX2X-ray1.90B/D/F/H12-20[»]
3AX3X-ray2.10B/D/F/H12-20[»]
3AX5X-ray2.20B/D12-20[»]
ProteinModelPortaliP11884.
SMRiP11884. Positions 26-519.

Miscellaneous databases

EvolutionaryTraceiP11884.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiP11884.
KOiK00128.
PhylomeDBiP11884.

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.

P11884-1 [UniParc]FASTAAdd to Basket

« Hide

MLRAALSTAR RGPRLSRLLS AAATSAVPAP NQQPEVFCNQ IFINNEWHDA    50
VSKKTFPTVN PSTGEVICQV AEGNKEDVDK AVKAAQAAFQ LGSPWRRMDA 100
SDRGRLLYRL ADLIERDRTY LAALETLDNG KPYVISYLVD LDMVLKCLRY 150
YAGWADKYHG KTIPIDGDFF SYTRHEPVGV CGQIIPWNFP LLMQAWKLGP 200
ALATGNVVVM KVAEQTPLTA LYVANLIKEA GFPPGVVNIV PGFGPTAGAA 250
IASHEDVDKV AFTGSTEVGH LIQVAAGSSN LKRVTLELGG KSPNIIMSDA 300
DMDWAVEQAH FALFFNQGQC CCAGSRTFVQ EDVYDEFVER SVARAKSRVV 350
GNPFDSRTEQ GPQVDETQFK KILGYIKSGQ QEGAKLLCGG GAAADRGYFI 400
QPTVFGDVKD GMTIAKEEIF GPVMQILKFK TIEEVVGRAN NSKYGLAAAV 450
FTKDLDKANY LSQALQAGTV WINCYDVFGA QSPFGGYKMS GSGRELGEYG 500
LQAYTEVKTV TVKVPQKNS 519
Length:519
Mass (Da):56,488
Last modified:October 1, 1989 - v1
Checksum:i75C748202F1333E5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti86 – 861Q → R in allele Aldh2*2 and allele Aldh2*3; in strains UChA and UChB. 1 Publication
Natural varianti498 – 4981E → K in allele Aldh2*3; in strain UChB. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14977 mRNA. Translation: CAA33101.1.
BC062081 mRNA. Translation: AAH62081.1.
M19030 mRNA. Translation: AAA40719.1.
AY566467 mRNA. Translation: AAS75813.1.
AY566468 mRNA. Translation: AAS75814.1.
AY566469 mRNA. Translation: AAS75815.1.
AF529165 mRNA. Translation: AAM94394.2.
AY034137 Genomic DNA. Translation: AAK57732.1.
PIRiS03564.
RefSeqiNP_115792.1. NM_032416.1.
UniGeneiRn.101781.

Genome annotation databases

GeneIDi29539.
KEGGirno:29539.
UCSCiRGD:69219. rat.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14977 mRNA. Translation: CAA33101.1 .
BC062081 mRNA. Translation: AAH62081.1 .
M19030 mRNA. Translation: AAA40719.1 .
AY566467 mRNA. Translation: AAS75813.1 .
AY566468 mRNA. Translation: AAS75814.1 .
AY566469 mRNA. Translation: AAS75815.1 .
AF529165 mRNA. Translation: AAM94394.2 .
AY034137 Genomic DNA. Translation: AAK57732.1 .
PIRi S03564.
RefSeqi NP_115792.1. NM_032416.1.
UniGenei Rn.101781.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OM2 NMR - B 12-20 [» ]
2V1S X-ray 2.05 H/I/J/K/L/M/N 12-24 [» ]
2V1T X-ray 1.92 C/D 12-22 [» ]
3AWR X-ray 2.00 C/D 12-20 [» ]
3AX2 X-ray 1.90 B/D/F/H 12-20 [» ]
3AX3 X-ray 2.10 B/D/F/H 12-20 [» ]
3AX5 X-ray 2.20 B/D 12-20 [» ]
ProteinModelPortali P11884.
SMRi P11884. Positions 26-519.
ModBasei Search...

Protein-protein interaction databases

IntActi P11884. 2 interactions.
MINTi MINT-4569918.

Chemistry

BindingDBi P11884.
ChEMBLi CHEMBL2812.
GuidetoPHARMACOLOGYi 2595.

PTM databases

PhosphoSitei P11884.

2D gel databases

World-2DPAGE 0004:P11884.

Proteomic databases

PaxDbi P11884.
PRIDEi P11884.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 29539.
KEGGi rno:29539.
UCSCi RGD:69219. rat.

Organism-specific databases

CTDi 217.
RGDi 69219. Aldh2.

Phylogenomic databases

eggNOGi COG1012.
HOGENOMi HOG000271505.
HOVERGENi HBG000097.
InParanoidi P11884.
KOi K00128.
PhylomeDBi P11884.

Enzyme and pathway databases

UniPathwayi UPA00780 ; UER00768 .
SABIO-RK P11884.

Miscellaneous databases

EvolutionaryTracei P11884.
NextBioi 609531.

Gene expression databases

Genevestigatori P11884.

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. "Primary structures of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences."
    Farres J., Guan K.-L., Weiner H.
    Eur. J. Biochem. 180:67-74(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "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.
  3. "Sequence of the signal peptide for rat liver mitochondrial aldehyde dehydrogenase."
    Farres J., Guan K.-L., Weiner H.
    Biochem. Biophys. Res. Commun. 150:1083-1087(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-29.
    Tissue: Liver.
  4. "Purification and characterization of catalytically active precursor of rat liver mitochondrial aldehyde dehydrogenase expressed in Escherichia coli."
    Jeng J., Weiner H.
    Arch. Biochem. Biophys. 289:214-222(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-19.
    Tissue: Liver.
  5. "Mutations in mitochondrial aldehyde dehydrogenase (ALDH2) change cofactor affinity and segregate with voluntary alcohol consumption in rats."
    Sapag A., Tampier L., Valle-Prieto A., Quintanilla M.E., Moncada C., Israel Y.
    Pharmacogenetics 13:509-515(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-519, VARIANTS ARG-86 AND LYS-498.
    Strain: UChA, UChB and Wistar.
    Tissue: Liver.
  6. "Genomic structure and sequence of the mitochondrial aldehyde dehydrogenase gene (ALDH2) of the Lewis rat."
    Sapag A., Urra S., Gonzalez-Jara F., Moncada C., Israel Y.
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-519.
    Strain: Lewis.
  7. "Genomic structure and sequence of the mitochondrial aldehyde dehydrogenase gene of the Lewis rat."
    Sapag A., Urra S., Gonzalez-Jara F., Moncada C., Israel Y.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-519.
    Strain: Lewis.
    Tissue: Liver.
  8. Lubec G., Afjehi-Sadat L., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 162-174; 198-228; 260-340; 327-340; 358-370; 397-409 AND 495-508, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Spinal cord.
  9. "A mitochondrial protein fraction catalyzing transport of the K+ analog T1+."
    Diwan J.J., Paliwal R., Kaftan E., Bawa R.
    FEBS Lett. 273:215-218(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 327-340.
  10. "Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20."
    Abe Y., Shodai T., Muto T., Mihara K., Torii H., Nishikawa S., Endo T., Kohda D.
    Cell 100:551-560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 12-22.

Entry informationi

Entry nameiALDH2_RAT
AccessioniPrimary (citable) accession number: P11884
Secondary accession number(s): Q6Q288
, Q6Q289, Q6Q290, Q8K3V8, Q91ZD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: September 3, 2014
This is version 139 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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